33 results on '"Cajic, S."'
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2. FUT6 deficiency compromises basophil function by selectively abrogating their sialyl-Lewis x expression
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Puan, K., San Luis, B., Yusof, N., Kumar, D., Andiappan, A., Lee, W., Cajic, S., Vuckovic, D., Chan, J., Döllner, T., Hou, H., Jiang, Y., Tian, C., Agee, M., Aslibekyan, S., Auton, A., Babalola, E., Bell, R., Bielenberg, J., Bryc, K., Bullis, E., Cameron, B., Coker, D., Partida, G., Dhamija, D., Das, S., Elson, S., Filshtein, T., Fletez-Brant, K., Fontanillas, P., Freyman, W., Gandhi, P., Heilbron, K., Hicks, B., Hinds, D., Huber, K., Jewett, E., Kleinman, A., Kukar, K., Lane, V., Lin, K., Lowe, M., Luff, M., McCreight, J., McIntyre, M., McManus, K., Micheletti, S., Moreno, M., Mountain, J., Mozaffari, S., Nandakumar, P., Noblin, E., O’Connell, J., Petrakovitz, A., Poznik, G., Schumacher, M., Shastri, A., Shelton, J., Shi, J., Shringarpure, S., Tran, V., Tung, J., Wang, X., Wang, W., Weldon, C., Wilton, P., Rapp, E., Poidinger, M., Wang, D., Soranzo, N., Lee, B., Rötzschke, O., Puan, Kia Joo [0000-0003-2445-3154], Kumar, Dilip [0000-0002-1848-3034], Andiappan, Anand Kumar [0000-0002-8442-1544], Cajic, Samanta [0000-0001-5820-0732], Chan, Jing De [0000-0002-2249-5273], Hou, Han Wei [0000-0001-6631-6321], Rapp, Erdmann [0000-0001-6618-2626], Poidinger, Michael [0000-0002-1047-2277], Soranzo, Nicole [0000-0003-1095-3852], Rötzschke, Olaf [0000-0001-8336-5248], Apollo - University of Cambridge Repository, Lee Kong Chian School of Medicine (LKCMedicine), and School of Mechanical and Aerospace Engineering
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0301 basic medicine ,Fucosyltransferase ,Allergy ,QH301-705.5 ,Population ,Medicine (miscellaneous) ,T-Cells ,Genetic predisposition to disease ,Gene Expression ,Basophil ,Immunoglobulin E ,Polymorphism, Single Nucleotide ,General Biochemistry, Genetics and Molecular Biology ,Article ,Cohort Studies ,03 medical and health sciences ,chemistry.chemical_compound ,Leukocyte Count ,0302 clinical medicine ,Sequence Homology, Nucleic Acid ,medicine ,Humans ,Medicine [Science] ,Leukocyte Rolling ,Biology (General) ,education ,Sialyl Lewis X Antigen ,Cells, Cultured ,education.field_of_study ,biology ,Base Sequence ,Gene Expression Profiling ,Mast-Cells ,Eosinophil ,Mast cell ,Fucosyltransferases ,Molecular biology ,Null allele ,Basophils ,030104 developmental biology ,medicine.anatomical_structure ,Sialyl-Lewis X ,chemistry ,030220 oncology & carcinogenesis ,biology.protein ,Mechanical engineering [Engineering] ,General Agricultural and Biological Sciences ,E-Selectin - Abstract
Sialyl-Lewis x (sLex, CD15s) is a tetra-saccharide on the surface of leukocytes required for E-selectin-mediated rolling, a prerequisite for leukocytes to migrate out of the blood vessels. Here we show using flow cytometry that sLex expression on basophils and mast cell progenitors depends on fucosyltransferase 6 (FUT6). Using genetic association data analysis and qPCR, the cell type-specific defect was associated with single nucleotide polymorphisms (SNPs) in the FUT6 gene region (tagged by rs17855739 and rs778798), affecting coding sequence and/or expression level of the mRNA. Heterozygous individuals with one functional FUT6 gene harbor a mixed population of sLex+ and sLex- basophils, a phenomenon caused by random monoallelic expression (RME). Microfluidic assay demonstrated FUT6-deficient basophils rolling on E-selectin is severely impaired. FUT6 null alleles carriers exhibit elevated blood basophil counts and a reduced itch sensitivity against insect bites. FUT6-deficiency thus dampens the basophil-mediated allergic response in the periphery, evident also in lower IgE titers and reduced eosinophil counts., Puan and San Luis et al. find that FUT6, encoding a fucosyltransferase, is required for the “rolling” behavior of certain white blood cells that enables them to move from blood vessels to tissues. They show that FUT6 deficiency leads to a loss of the tetrasaccharide sLex on the surface of basophils, resulting in cells that are less sticky and therefore less able to form the necessary adhesions for exiting the blood vessel to drive the allergic reaction.
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- 2021
3. Advances in the Chemical Synthesis of Carbohydrates and Glycoconjugates
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Malik, Ankita, Seeberger, Peter H., Varón Silva, Daniel, Scheper, Thomas, Series Editor, Belkin, Shimshon, Editorial Board Member, Bley, Thomas, Editorial Board Member, Bohlmann, Jörg, Editorial Board Member, Gu, Man Bock, Editorial Board Member, Hu, Wei-Shou, Editorial Board Member, Mattiasson, Bo, Editorial Board Member, Olsson, Lisbeth, Editorial Board Member, Seitz, Harald, Editorial Board Member, Silva, Ana Catarina, Editorial Board Member, Ulber, Roland, Editorial Board Member, Zeng, An-Ping, Editorial Board Member, Zhong, Jian-Jiang, Editorial Board Member, Zhou, Weichang, Editorial Board Member, Rapp, Erdmann, editor, Reichl, Udo, editor, Alagesan, K., With Contri.By, Betenbaugh, M. J., With Contri.By, Butler, M., With Contri.By, Buyel, J. F., With Contri.By, Cajic, S., With Contri.By, Callewaert, N., With Contri.By, Can, Ö., With Contri.By, Cox, M. M. J., With Contri.By, DeLisa, M. P., With Contri.By, De Wachter, C., With Contri.By, Elling, L., With Contri.By, Fischer, R., With Contri.By, Flitsch, S. L., With Contri.By, Frohnmeyer, H., With Contri.By, Gottschalk, J., With Contri.By, Goyette-Desjardins, G., With Contri.By, Heffner, K. M., With Contri.By, Hizal, D. B., With Contri.By, Hoffmann, M., With Contri.By, Holland, T., With Contri.By, Jefferis, R., With Contri.By, Kolarich, D., With Contri.By, Laaf, D., With Contri.By, Lepenies, B., With Contri.By, Malik, A., With Contri.By, Martinez, J. E. R., With Contri.By, Mills, D. C., With Contri.By, Moeller, T. D., With Contri.By, Palomares, L. A., With Contri.By, Pralow, A., With Contri.By, RamÚrez, O. T., With Contri.By, Rapp, E., With Contri.By, Reichl, U., With Contri.By, Rexer, T., With Contri.By, Sack, M., With Contri.By, Schillberg, S., With Contri.By, Schön, K., With Contri.By, Seeberger, P. H., With Contri.By, Srivastava, I. K., With Contri.By, Stoger, E., With Contri.By, Thomas, B., With Contri.By, Twyman, R. M., With Contri.By, Van Landuyt, L., With Contri.By, Varón Silva, D., With Contri.By, Wang, Q., With Contri.By, Weyant, K. B., With Contri.By, and Yates, L. E., With Contri.By
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- 2021
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4. Enzymatic Synthesis of Glycans and Glycoconjugates
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Rexer, Thomas, Laaf, Dominic, Gottschalk, Johannes, Frohnmeyer, Hannes, Rapp, Erdmann, Elling, Lothar, Scheper, Thomas, Series Editor, Belkin, Shimshon, Editorial Board Member, Bley, Thomas, Editorial Board Member, Bohlmann, Jörg, Editorial Board Member, Gu, Man Bock, Editorial Board Member, Hu, Wei-Shou, Editorial Board Member, Mattiasson, Bo, Editorial Board Member, Olsson, Lisbeth, Editorial Board Member, Seitz, Harald, Editorial Board Member, Silva, Ana Catarina, Editorial Board Member, Ulber, Roland, Editorial Board Member, Zeng, An-Ping, Editorial Board Member, Zhong, Jian-Jiang, Editorial Board Member, Zhou, Weichang, Editorial Board Member, Rapp, Erdmann, editor, Reichl, Udo, editor, Alagesan, K., With Contri.By, Betenbaugh, M. J., With Contri.By, Butler, M., With Contri.By, Buyel, J. F., With Contri.By, Cajic, S., With Contri.By, Callewaert, N., With Contri.By, Can, Ö., With Contri.By, Cox, M. M. J., With Contri.By, DeLisa, M. P., With Contri.By, De Wachter, C., With Contri.By, Elling, L., With Contri.By, Fischer, R., With Contri.By, Flitsch, S. L., With Contri.By, Frohnmeyer, H., With Contri.By, Gottschalk, J., With Contri.By, Goyette-Desjardins, G., With Contri.By, Heffner, K. M., With Contri.By, Hizal, D. B., With Contri.By, Hoffmann, M., With Contri.By, Holland, T., With Contri.By, Jefferis, R., With Contri.By, Kolarich, D., With Contri.By, Laaf, D., With Contri.By, Lepenies, B., With Contri.By, Malik, A., With Contri.By, Martinez, J. E. R., With Contri.By, Mills, D. C., With Contri.By, Moeller, T. D., With Contri.By, Palomares, L. A., With Contri.By, Pralow, A., With Contri.By, RamÚrez, O. T., With Contri.By, Rapp, E., With Contri.By, Reichl, U., With Contri.By, Rexer, T., With Contri.By, Sack, M., With Contri.By, Schillberg, S., With Contri.By, Schön, K., With Contri.By, Seeberger, P. H., With Contri.By, Srivastava, I. K., With Contri.By, Stoger, E., With Contri.By, Thomas, B., With Contri.By, Twyman, R. M., With Contri.By, Van Landuyt, L., With Contri.By, Varón Silva, D., With Contri.By, Wang, Q., With Contri.By, Weyant, K. B., With Contri.By, and Yates, L. E., With Contri.By
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- 2021
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5. Interplay of Carbohydrate and Carrier in Antibacterial Glycoconjugate Vaccines
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Moeller, Tyler D., Weyant, Kevin B., DeLisa, Matthew P., Scheper, Thomas, Series Editor, Belkin, Shimshon, Editorial Board Member, Bley, Thomas, Editorial Board Member, Bohlmann, Jörg, Editorial Board Member, Gu, Man Bock, Editorial Board Member, Hu, Wei-Shou, Editorial Board Member, Mattiasson, Bo, Editorial Board Member, Olsson, Lisbeth, Editorial Board Member, Seitz, Harald, Editorial Board Member, Silva, Ana Catarina, Editorial Board Member, Ulber, Roland, Editorial Board Member, Zeng, An-Ping, Editorial Board Member, Zhong, Jian-Jiang, Editorial Board Member, Zhou, Weichang, Editorial Board Member, Rapp, Erdmann, editor, Reichl, Udo, editor, Alagesan, K., With Contri.By, Betenbaugh, M. J., With Contri.By, Butler, M., With Contri.By, Buyel, J. F., With Contri.By, Cajic, S., With Contri.By, Callewaert, N., With Contri.By, Can, Ö., With Contri.By, Cox, M. M. J., With Contri.By, DeLisa, M. P., With Contri.By, De Wachter, C., With Contri.By, Elling, L., With Contri.By, Fischer, R., With Contri.By, Flitsch, S. L., With Contri.By, Frohnmeyer, H., With Contri.By, Gottschalk, J., With Contri.By, Goyette-Desjardins, G., With Contri.By, Heffner, K. M., With Contri.By, Hizal, D. B., With Contri.By, Hoffmann, M., With Contri.By, Holland, T., With Contri.By, Jefferis, R., With Contri.By, Kolarich, D., With Contri.By, Laaf, D., With Contri.By, Lepenies, B., With Contri.By, Malik, A., With Contri.By, Martinez, J. E. R., With Contri.By, Mills, D. C., With Contri.By, Moeller, T. D., With Contri.By, Palomares, L. A., With Contri.By, Pralow, A., With Contri.By, RamÚrez, O. T., With Contri.By, Rapp, E., With Contri.By, Reichl, U., With Contri.By, Rexer, T., With Contri.By, Sack, M., With Contri.By, Schillberg, S., With Contri.By, Schön, K., With Contri.By, Seeberger, P. H., With Contri.By, Srivastava, I. K., With Contri.By, Stoger, E., With Contri.By, Thomas, B., With Contri.By, Twyman, R. M., With Contri.By, Van Landuyt, L., With Contri.By, Varón Silva, D., With Contri.By, Wang, Q., With Contri.By, Weyant, K. B., With Contri.By, and Yates, L. E., With Contri.By
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- 2021
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6. Glyco-Engineering of Plant-Based Expression Systems
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Fischer, Rainer, Holland, Tanja, Sack, Markus, Schillberg, Stefan, Stoger, Eva, Twyman, Richard M., Buyel, Johannes F., Scheper, Thomas, Series Editor, Belkin, Shimshon, Editorial Board Member, Bley, Thomas, Editorial Board Member, Bohlmann, Jörg, Editorial Board Member, Gu, Man Bock, Editorial Board Member, Hu, Wei-Shou, Editorial Board Member, Mattiasson, Bo, Editorial Board Member, Olsson, Lisbeth, Editorial Board Member, Seitz, Harald, Editorial Board Member, Silva, Ana Catarina, Editorial Board Member, Ulber, Roland, Editorial Board Member, Zeng, An-Ping, Editorial Board Member, Zhong, Jian-Jiang, Editorial Board Member, Zhou, Weichang, Editorial Board Member, Rapp, Erdmann, editor, Reichl, Udo, editor, Alagesan, K., With Contri.By, Betenbaugh, M. J., With Contri.By, Butler, M., With Contri.By, Buyel, J. F., With Contri.By, Cajic, S., With Contri.By, Callewaert, N., With Contri.By, Can, Ö., With Contri.By, Cox, M. M. J., With Contri.By, DeLisa, M. P., With Contri.By, De Wachter, C., With Contri.By, Elling, L., With Contri.By, Fischer, R., With Contri.By, Flitsch, S. L., With Contri.By, Frohnmeyer, H., With Contri.By, Gottschalk, J., With Contri.By, Goyette-Desjardins, G., With Contri.By, Heffner, K. M., With Contri.By, Hizal, D. B., With Contri.By, Hoffmann, M., With Contri.By, Holland, T., With Contri.By, Jefferis, R., With Contri.By, Kolarich, D., With Contri.By, Laaf, D., With Contri.By, Lepenies, B., With Contri.By, Malik, A., With Contri.By, Martinez, J. E. R., With Contri.By, Mills, D. C., With Contri.By, Moeller, T. D., With Contri.By, Palomares, L. A., With Contri.By, Pralow, A., With Contri.By, RamÚrez, O. T., With Contri.By, Rapp, E., With Contri.By, Reichl, U., With Contri.By, Rexer, T., With Contri.By, Sack, M., With Contri.By, Schillberg, S., With Contri.By, Schön, K., With Contri.By, Seeberger, P. H., With Contri.By, Srivastava, I. K., With Contri.By, Stoger, E., With Contri.By, Thomas, B., With Contri.By, Twyman, R. M., With Contri.By, Van Landuyt, L., With Contri.By, Varón Silva, D., With Contri.By, Wang, Q., With Contri.By, Weyant, K. B., With Contri.By, and Yates, L. E., With Contri.By
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- 2021
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7. Engineering of Yeast Glycoprotein Expression
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De Wachter, Charlot, Van Landuyt, Linde, Callewaert, Nico, Scheper, Thomas, Series Editor, Belkin, Shimshon, Editorial Board Member, Bley, Thomas, Editorial Board Member, Bohlmann, Jörg, Editorial Board Member, Gu, Man Bock, Editorial Board Member, Hu, Wei-Shou, Editorial Board Member, Mattiasson, Bo, Editorial Board Member, Olsson, Lisbeth, Editorial Board Member, Seitz, Harald, Editorial Board Member, Silva, Ana Catarina, Editorial Board Member, Ulber, Roland, Editorial Board Member, Zeng, An-Ping, Editorial Board Member, Zhong, Jian-Jiang, Editorial Board Member, Zhou, Weichang, Editorial Board Member, Rapp, Erdmann, editor, Reichl, Udo, editor, Alagesan, K., With Contri.By, Betenbaugh, M. J., With Contri.By, Butler, M., With Contri.By, Buyel, J. F., With Contri.By, Cajic, S., With Contri.By, Callewaert, N., With Contri.By, Can, Ö., With Contri.By, Cox, M. M. J., With Contri.By, DeLisa, M. P., With Contri.By, De Wachter, C., With Contri.By, Elling, L., With Contri.By, Fischer, R., With Contri.By, Flitsch, S. L., With Contri.By, Frohnmeyer, H., With Contri.By, Gottschalk, J., With Contri.By, Goyette-Desjardins, G., With Contri.By, Heffner, K. M., With Contri.By, Hizal, D. B., With Contri.By, Hoffmann, M., With Contri.By, Holland, T., With Contri.By, Jefferis, R., With Contri.By, Kolarich, D., With Contri.By, Laaf, D., With Contri.By, Lepenies, B., With Contri.By, Malik, A., With Contri.By, Martinez, J. E. R., With Contri.By, Mills, D. C., With Contri.By, Moeller, T. D., With Contri.By, Palomares, L. A., With Contri.By, Pralow, A., With Contri.By, RamÚrez, O. T., With Contri.By, Rapp, E., With Contri.By, Reichl, U., With Contri.By, Rexer, T., With Contri.By, Sack, M., With Contri.By, Schillberg, S., With Contri.By, Schön, K., With Contri.By, Seeberger, P. H., With Contri.By, Srivastava, I. K., With Contri.By, Stoger, E., With Contri.By, Thomas, B., With Contri.By, Twyman, R. M., With Contri.By, Van Landuyt, L., With Contri.By, Varón Silva, D., With Contri.By, Wang, Q., With Contri.By, Weyant, K. B., With Contri.By, and Yates, L. E., With Contri.By
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- 2021
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8. Bacterial Glycoengineering as a Biosynthetic Route to Customized Glycomolecules
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Yates, Laura E., Mills, Dominic C., DeLisa, Matthew P., Scheper, Thomas, Series Editor, Belkin, Shimshon, Editorial Board Member, Bley, Thomas, Editorial Board Member, Bohlmann, Jörg, Editorial Board Member, Gu, Man Bock, Editorial Board Member, Hu, Wei-Shou, Editorial Board Member, Mattiasson, Bo, Editorial Board Member, Olsson, Lisbeth, Editorial Board Member, Seitz, Harald, Editorial Board Member, Silva, Ana Catarina, Editorial Board Member, Ulber, Roland, Editorial Board Member, Zeng, An-Ping, Editorial Board Member, Zhong, Jian-Jiang, Editorial Board Member, Zhou, Weichang, Editorial Board Member, Rapp, Erdmann, editor, Reichl, Udo, editor, Alagesan, K., With Contri.By, Betenbaugh, M. J., With Contri.By, Butler, M., With Contri.By, Buyel, J. F., With Contri.By, Cajic, S., With Contri.By, Callewaert, N., With Contri.By, Can, Ö., With Contri.By, Cox, M. M. J., With Contri.By, DeLisa, M. P., With Contri.By, De Wachter, C., With Contri.By, Elling, L., With Contri.By, Fischer, R., With Contri.By, Flitsch, S. L., With Contri.By, Frohnmeyer, H., With Contri.By, Gottschalk, J., With Contri.By, Goyette-Desjardins, G., With Contri.By, Heffner, K. M., With Contri.By, Hizal, D. B., With Contri.By, Hoffmann, M., With Contri.By, Holland, T., With Contri.By, Jefferis, R., With Contri.By, Kolarich, D., With Contri.By, Laaf, D., With Contri.By, Lepenies, B., With Contri.By, Malik, A., With Contri.By, Martinez, J. E. R., With Contri.By, Mills, D. C., With Contri.By, Moeller, T. D., With Contri.By, Palomares, L. A., With Contri.By, Pralow, A., With Contri.By, RamÚrez, O. T., With Contri.By, Rapp, E., With Contri.By, Reichl, U., With Contri.By, Rexer, T., With Contri.By, Sack, M., With Contri.By, Schillberg, S., With Contri.By, Schön, K., With Contri.By, Seeberger, P. H., With Contri.By, Srivastava, I. K., With Contri.By, Stoger, E., With Contri.By, Thomas, B., With Contri.By, Twyman, R. M., With Contri.By, Van Landuyt, L., With Contri.By, Varón Silva, D., With Contri.By, Wang, Q., With Contri.By, Weyant, K. B., With Contri.By, and Yates, L. E., With Contri.By
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- 2021
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9. Recombinant Proteins and Monoclonal Antibodies
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Jefferis, Roy, Scheper, Thomas, Series Editor, Belkin, Shimshon, Editorial Board Member, Bley, Thomas, Editorial Board Member, Bohlmann, Jörg, Editorial Board Member, Gu, Man Bock, Editorial Board Member, Hu, Wei-Shou, Editorial Board Member, Mattiasson, Bo, Editorial Board Member, Olsson, Lisbeth, Editorial Board Member, Seitz, Harald, Editorial Board Member, Silva, Ana Catarina, Editorial Board Member, Ulber, Roland, Editorial Board Member, Zeng, An-Ping, Editorial Board Member, Zhong, Jian-Jiang, Editorial Board Member, Zhou, Weichang, Editorial Board Member, Rapp, Erdmann, editor, Reichl, Udo, editor, Alagesan, K., With Contri.By, Betenbaugh, M. J., With Contri.By, Butler, M., With Contri.By, Buyel, J. F., With Contri.By, Cajic, S., With Contri.By, Callewaert, N., With Contri.By, Can, Ö., With Contri.By, Cox, M. M. J., With Contri.By, DeLisa, M. P., With Contri.By, De Wachter, C., With Contri.By, Elling, L., With Contri.By, Fischer, R., With Contri.By, Flitsch, S. L., With Contri.By, Frohnmeyer, H., With Contri.By, Gottschalk, J., With Contri.By, Goyette-Desjardins, G., With Contri.By, Heffner, K. M., With Contri.By, Hizal, D. B., With Contri.By, Hoffmann, M., With Contri.By, Holland, T., With Contri.By, Jefferis, R., With Contri.By, Kolarich, D., With Contri.By, Laaf, D., With Contri.By, Lepenies, B., With Contri.By, Malik, A., With Contri.By, Martinez, J. E. R., With Contri.By, Mills, D. C., With Contri.By, Moeller, T. D., With Contri.By, Palomares, L. A., With Contri.By, Pralow, A., With Contri.By, RamÚrez, O. T., With Contri.By, Rapp, E., With Contri.By, Reichl, U., With Contri.By, Rexer, T., With Contri.By, Sack, M., With Contri.By, Schillberg, S., With Contri.By, Schön, K., With Contri.By, Seeberger, P. H., With Contri.By, Srivastava, I. K., With Contri.By, Stoger, E., With Contri.By, Thomas, B., With Contri.By, Twyman, R. M., With Contri.By, Van Landuyt, L., With Contri.By, Varón Silva, D., With Contri.By, Wang, Q., With Contri.By, Weyant, K. B., With Contri.By, and Yates, L. E., With Contri.By
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- 2021
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10. Glycobiotechnology of the Insect Cell-Baculovirus Expression System Technology
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Palomares, Laura A., Srivastava, Indresh K., Ramírez, Octavio T., Cox, Manon M. J., Scheper, Thomas, Series Editor, Belkin, Shimshon, Editorial Board Member, Bley, Thomas, Editorial Board Member, Bohlmann, Jörg, Editorial Board Member, Gu, Man Bock, Editorial Board Member, Hu, Wei-Shou, Editorial Board Member, Mattiasson, Bo, Editorial Board Member, Olsson, Lisbeth, Editorial Board Member, Seitz, Harald, Editorial Board Member, Silva, Ana Catarina, Editorial Board Member, Ulber, Roland, Editorial Board Member, Zeng, An-Ping, Editorial Board Member, Zhong, Jian-Jiang, Editorial Board Member, Zhou, Weichang, Editorial Board Member, Rapp, Erdmann, editor, Reichl, Udo, editor, Alagesan, K., With Contri.By, Betenbaugh, M. J., With Contri.By, Butler, M., With Contri.By, Buyel, J. F., With Contri.By, Cajic, S., With Contri.By, Callewaert, N., With Contri.By, Can, Ö., With Contri.By, Cox, M. M. J., With Contri.By, DeLisa, M. P., With Contri.By, De Wachter, C., With Contri.By, Elling, L., With Contri.By, Fischer, R., With Contri.By, Flitsch, S. L., With Contri.By, Frohnmeyer, H., With Contri.By, Gottschalk, J., With Contri.By, Goyette-Desjardins, G., With Contri.By, Heffner, K. M., With Contri.By, Hizal, D. B., With Contri.By, Hoffmann, M., With Contri.By, Holland, T., With Contri.By, Jefferis, R., With Contri.By, Kolarich, D., With Contri.By, Laaf, D., With Contri.By, Lepenies, B., With Contri.By, Malik, A., With Contri.By, Martinez, J. E. R., With Contri.By, Mills, D. C., With Contri.By, Moeller, T. D., With Contri.By, Palomares, L. A., With Contri.By, Pralow, A., With Contri.By, RamÚrez, O. T., With Contri.By, Rapp, E., With Contri.By, Reichl, U., With Contri.By, Rexer, T., With Contri.By, Sack, M., With Contri.By, Schillberg, S., With Contri.By, Schön, K., With Contri.By, Seeberger, P. H., With Contri.By, Srivastava, I. K., With Contri.By, Stoger, E., With Contri.By, Thomas, B., With Contri.By, Twyman, R. M., With Contri.By, Van Landuyt, L., With Contri.By, Varón Silva, D., With Contri.By, Wang, Q., With Contri.By, Weyant, K. B., With Contri.By, and Yates, L. E., With Contri.By
- Published
- 2021
- Full Text
- View/download PDF
11. Animal Cell Expression Systems
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Butler, M., Reichl, U., Scheper, Thomas, Series Editor, Belkin, Shimshon, Editorial Board Member, Bley, Thomas, Editorial Board Member, Bohlmann, Jörg, Editorial Board Member, Gu, Man Bock, Editorial Board Member, Hu, Wei-Shou, Editorial Board Member, Mattiasson, Bo, Editorial Board Member, Olsson, Lisbeth, Editorial Board Member, Seitz, Harald, Editorial Board Member, Silva, Ana Catarina, Editorial Board Member, Ulber, Roland, Editorial Board Member, Zeng, An-Ping, Editorial Board Member, Zhong, Jian-Jiang, Editorial Board Member, Zhou, Weichang, Editorial Board Member, Rapp, Erdmann, editor, Reichl, Udo, editor, Alagesan, K., With Contri.By, Betenbaugh, M. J., With Contri.By, Butler, M., With Contri.By, Buyel, J. F., With Contri.By, Cajic, S., With Contri.By, Callewaert, N., With Contri.By, Can, Ö., With Contri.By, Cox, M. M. J., With Contri.By, DeLisa, M. P., With Contri.By, De Wachter, C., With Contri.By, Elling, L., With Contri.By, Fischer, R., With Contri.By, Flitsch, S. L., With Contri.By, Frohnmeyer, H., With Contri.By, Gottschalk, J., With Contri.By, Goyette-Desjardins, G., With Contri.By, Heffner, K. M., With Contri.By, Hizal, D. B., With Contri.By, Hoffmann, M., With Contri.By, Holland, T., With Contri.By, Jefferis, R., With Contri.By, Kolarich, D., With Contri.By, Laaf, D., With Contri.By, Lepenies, B., With Contri.By, Malik, A., With Contri.By, Martinez, J. E. R., With Contri.By, Mills, D. C., With Contri.By, Moeller, T. D., With Contri.By, Palomares, L. A., With Contri.By, Pralow, A., With Contri.By, RamÚrez, O. T., With Contri.By, Rapp, E., With Contri.By, Reichl, U., With Contri.By, Rexer, T., With Contri.By, Sack, M., With Contri.By, Schillberg, S., With Contri.By, Schön, K., With Contri.By, Seeberger, P. H., With Contri.By, Srivastava, I. K., With Contri.By, Stoger, E., With Contri.By, Thomas, B., With Contri.By, Twyman, R. M., With Contri.By, Van Landuyt, L., With Contri.By, Varón Silva, D., With Contri.By, Wang, Q., With Contri.By, Weyant, K. B., With Contri.By, and Yates, L. E., With Contri.By
- Published
- 2021
- Full Text
- View/download PDF
12. Glycoengineering of Mammalian Expression Systems on a Cellular Level
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Heffner, Kelley M., Wang, Qiong, Hizal, Deniz Baycin, Can, Özge, Betenbaugh, Michael J., Scheper, Thomas, Series Editor, Belkin, Shimshon, Editorial Board Member, Bley, Thomas, Editorial Board Member, Bohlmann, Jörg, Editorial Board Member, Gu, Man Bock, Editorial Board Member, Hu, Wei-Shou, Editorial Board Member, Mattiasson, Bo, Editorial Board Member, Olsson, Lisbeth, Editorial Board Member, Seitz, Harald, Editorial Board Member, Silva, Ana Catarina, Editorial Board Member, Ulber, Roland, Editorial Board Member, Zeng, An-Ping, Editorial Board Member, Zhong, Jian-Jiang, Editorial Board Member, Zhou, Weichang, Editorial Board Member, Rapp, Erdmann, editor, Reichl, Udo, editor, Alagesan, K., With Contri.By, Betenbaugh, M. J., With Contri.By, Butler, M., With Contri.By, Buyel, J. F., With Contri.By, Cajic, S., With Contri.By, Callewaert, N., With Contri.By, Can, Ö., With Contri.By, Cox, M. M. J., With Contri.By, DeLisa, M. P., With Contri.By, De Wachter, C., With Contri.By, Elling, L., With Contri.By, Fischer, R., With Contri.By, Flitsch, S. L., With Contri.By, Frohnmeyer, H., With Contri.By, Gottschalk, J., With Contri.By, Goyette-Desjardins, G., With Contri.By, Heffner, K. M., With Contri.By, Hizal, D. B., With Contri.By, Hoffmann, M., With Contri.By, Holland, T., With Contri.By, Jefferis, R., With Contri.By, Kolarich, D., With Contri.By, Laaf, D., With Contri.By, Lepenies, B., With Contri.By, Malik, A., With Contri.By, Martinez, J. E. R., With Contri.By, Mills, D. C., With Contri.By, Moeller, T. D., With Contri.By, Palomares, L. A., With Contri.By, Pralow, A., With Contri.By, RamÚrez, O. T., With Contri.By, Rapp, E., With Contri.By, Reichl, U., With Contri.By, Rexer, T., With Contri.By, Sack, M., With Contri.By, Schillberg, S., With Contri.By, Schön, K., With Contri.By, Seeberger, P. H., With Contri.By, Srivastava, I. K., With Contri.By, Stoger, E., With Contri.By, Thomas, B., With Contri.By, Twyman, R. M., With Contri.By, Van Landuyt, L., With Contri.By, Varón Silva, D., With Contri.By, Wang, Q., With Contri.By, Weyant, K. B., With Contri.By, and Yates, L. E., With Contri.By
- Published
- 2021
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- View/download PDF
13. Glycoproteomics Technologies in Glycobiotechnology
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Alagesan, Kathirvel, Hoffmann, Marcus, Rapp, Erdmann, Kolarich, Daniel, Scheper, Thomas, Series Editor, Belkin, Shimshon, Editorial Board Member, Bley, Thomas, Editorial Board Member, Bohlmann, Jörg, Editorial Board Member, Gu, Man Bock, Editorial Board Member, Hu, Wei-Shou, Editorial Board Member, Mattiasson, Bo, Editorial Board Member, Olsson, Lisbeth, Editorial Board Member, Seitz, Harald, Editorial Board Member, Silva, Ana Catarina, Editorial Board Member, Ulber, Roland, Editorial Board Member, Zeng, An-Ping, Editorial Board Member, Zhong, Jian-Jiang, Editorial Board Member, Zhou, Weichang, Editorial Board Member, Rapp, Erdmann, editor, Reichl, Udo, editor, Alagesan, K., With Contri.By, Betenbaugh, M. J., With Contri.By, Butler, M., With Contri.By, Buyel, J. F., With Contri.By, Cajic, S., With Contri.By, Callewaert, N., With Contri.By, Can, Ö., With Contri.By, Cox, M. M. J., With Contri.By, DeLisa, M. P., With Contri.By, De Wachter, C., With Contri.By, Elling, L., With Contri.By, Fischer, R., With Contri.By, Flitsch, S. L., With Contri.By, Frohnmeyer, H., With Contri.By, Gottschalk, J., With Contri.By, Goyette-Desjardins, G., With Contri.By, Heffner, K. M., With Contri.By, Hizal, D. B., With Contri.By, Hoffmann, M., With Contri.By, Holland, T., With Contri.By, Jefferis, R., With Contri.By, Kolarich, D., With Contri.By, Laaf, D., With Contri.By, Lepenies, B., With Contri.By, Malik, A., With Contri.By, Martinez, J. E. R., With Contri.By, Mills, D. C., With Contri.By, Moeller, T. D., With Contri.By, Palomares, L. A., With Contri.By, Pralow, A., With Contri.By, RamÚrez, O. T., With Contri.By, Rapp, E., With Contri.By, Reichl, U., With Contri.By, Rexer, T., With Contri.By, Sack, M., With Contri.By, Schillberg, S., With Contri.By, Schön, K., With Contri.By, Seeberger, P. H., With Contri.By, Srivastava, I. K., With Contri.By, Stoger, E., With Contri.By, Thomas, B., With Contri.By, Twyman, R. M., With Contri.By, Van Landuyt, L., With Contri.By, Varón Silva, D., With Contri.By, Wang, Q., With Contri.By, Weyant, K. B., With Contri.By, and Yates, L. E., With Contri.By
- Published
- 2021
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14. State-of-the-Art Glycomics Technologies in Glycobiotechnology
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Pralow, Alexander, Cajic, Samanta, Alagesan, Kathirvel, Kolarich, Daniel, Rapp, Erdmann, Scheper, Thomas, Series Editor, Belkin, Shimshon, Editorial Board Member, Bley, Thomas, Editorial Board Member, Bohlmann, Jörg, Editorial Board Member, Gu, Man Bock, Editorial Board Member, Hu, Wei-Shou, Editorial Board Member, Mattiasson, Bo, Editorial Board Member, Olsson, Lisbeth, Editorial Board Member, Seitz, Harald, Editorial Board Member, Silva, Ana Catarina, Editorial Board Member, Ulber, Roland, Editorial Board Member, Zeng, An-Ping, Editorial Board Member, Zhong, Jian-Jiang, Editorial Board Member, Zhou, Weichang, Editorial Board Member, Rapp, Erdmann, editor, Reichl, Udo, editor, Alagesan, K., With Contri.By, Betenbaugh, M. J., With Contri.By, Butler, M., With Contri.By, Buyel, J. F., With Contri.By, Cajic, S., With Contri.By, Callewaert, N., With Contri.By, Can, Ö., With Contri.By, Cox, M. M. J., With Contri.By, DeLisa, M. P., With Contri.By, De Wachter, C., With Contri.By, Elling, L., With Contri.By, Fischer, R., With Contri.By, Flitsch, S. L., With Contri.By, Frohnmeyer, H., With Contri.By, Gottschalk, J., With Contri.By, Goyette-Desjardins, G., With Contri.By, Heffner, K. M., With Contri.By, Hizal, D. B., With Contri.By, Hoffmann, M., With Contri.By, Holland, T., With Contri.By, Jefferis, R., With Contri.By, Kolarich, D., With Contri.By, Laaf, D., With Contri.By, Lepenies, B., With Contri.By, Malik, A., With Contri.By, Martinez, J. E. R., With Contri.By, Mills, D. C., With Contri.By, Moeller, T. D., With Contri.By, Palomares, L. A., With Contri.By, Pralow, A., With Contri.By, RamÚrez, O. T., With Contri.By, Rapp, E., With Contri.By, Reichl, U., With Contri.By, Rexer, T., With Contri.By, Sack, M., With Contri.By, Schillberg, S., With Contri.By, Schön, K., With Contri.By, Seeberger, P. H., With Contri.By, Srivastava, I. K., With Contri.By, Stoger, E., With Contri.By, Thomas, B., With Contri.By, Twyman, R. M., With Contri.By, Van Landuyt, L., With Contri.By, Varón Silva, D., With Contri.By, Wang, Q., With Contri.By, Weyant, K. B., With Contri.By, and Yates, L. E., With Contri.By
- Published
- 2021
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15. Impact of Protein Glycosylation on the Design of Viral Vaccines
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Schön, Kathleen, Lepenies, Bernd, Goyette-Desjardins, Guillaume, Scheper, Thomas, Series Editor, Belkin, Shimshon, Editorial Board Member, Bley, Thomas, Editorial Board Member, Bohlmann, Jörg, Editorial Board Member, Gu, Man Bock, Editorial Board Member, Hu, Wei-Shou, Editorial Board Member, Mattiasson, Bo, Editorial Board Member, Olsson, Lisbeth, Editorial Board Member, Seitz, Harald, Editorial Board Member, Silva, Ana Catarina, Editorial Board Member, Ulber, Roland, Editorial Board Member, Zeng, An-Ping, Editorial Board Member, Zhong, Jian-Jiang, Editorial Board Member, Zhou, Weichang, Editorial Board Member, Rapp, Erdmann, editor, Reichl, Udo, editor, Alagesan, K., With Contri.By, Betenbaugh, M. J., With Contri.By, Butler, M., With Contri.By, Buyel, J. F., With Contri.By, Cajic, S., With Contri.By, Callewaert, N., With Contri.By, Can, Ö., With Contri.By, Cox, M. M. J., With Contri.By, DeLisa, M. P., With Contri.By, De Wachter, C., With Contri.By, Elling, L., With Contri.By, Fischer, R., With Contri.By, Flitsch, S. L., With Contri.By, Frohnmeyer, H., With Contri.By, Gottschalk, J., With Contri.By, Goyette-Desjardins, G., With Contri.By, Heffner, K. M., With Contri.By, Hizal, D. B., With Contri.By, Hoffmann, M., With Contri.By, Holland, T., With Contri.By, Jefferis, R., With Contri.By, Kolarich, D., With Contri.By, Laaf, D., With Contri.By, Lepenies, B., With Contri.By, Malik, A., With Contri.By, Martinez, J. E. R., With Contri.By, Mills, D. C., With Contri.By, Moeller, T. D., With Contri.By, Palomares, L. A., With Contri.By, Pralow, A., With Contri.By, RamÚrez, O. T., With Contri.By, Rapp, E., With Contri.By, Reichl, U., With Contri.By, Rexer, T., With Contri.By, Sack, M., With Contri.By, Schillberg, S., With Contri.By, Schön, K., With Contri.By, Seeberger, P. H., With Contri.By, Srivastava, I. K., With Contri.By, Stoger, E., With Contri.By, Thomas, B., With Contri.By, Twyman, R. M., With Contri.By, Van Landuyt, L., With Contri.By, Varón Silva, D., With Contri.By, Wang, Q., With Contri.By, Weyant, K. B., With Contri.By, and Yates, L. E., With Contri.By
- Published
- 2021
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16. Glycan Array Technology
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Martinez, Juana Elizabeth Reyes, Thomas, Baptiste, Flitsch, Sabine Lahja, Scheper, Thomas, Series Editor, Belkin, Shimshon, Editorial Board Member, Bley, Thomas, Editorial Board Member, Bohlmann, Jörg, Editorial Board Member, Gu, Man Bock, Editorial Board Member, Hu, Wei-Shou, Editorial Board Member, Mattiasson, Bo, Editorial Board Member, Olsson, Lisbeth, Editorial Board Member, Seitz, Harald, Editorial Board Member, Silva, Ana Catarina, Editorial Board Member, Ulber, Roland, Editorial Board Member, Zeng, An-Ping, Editorial Board Member, Zhong, Jian-Jiang, Editorial Board Member, Zhou, Weichang, Editorial Board Member, Rapp, Erdmann, editor, Reichl, Udo, editor, Alagesan, K., With Contri.By, Betenbaugh, M. J., With Contri.By, Butler, M., With Contri.By, Buyel, J. F., With Contri.By, Cajic, S., With Contri.By, Callewaert, N., With Contri.By, Can, Ö., With Contri.By, Cox, M. M. J., With Contri.By, DeLisa, M. P., With Contri.By, De Wachter, C., With Contri.By, Elling, L., With Contri.By, Fischer, R., With Contri.By, Flitsch, S. L., With Contri.By, Frohnmeyer, H., With Contri.By, Gottschalk, J., With Contri.By, Goyette-Desjardins, G., With Contri.By, Heffner, K. M., With Contri.By, Hizal, D. B., With Contri.By, Hoffmann, M., With Contri.By, Holland, T., With Contri.By, Jefferis, R., With Contri.By, Kolarich, D., With Contri.By, Laaf, D., With Contri.By, Lepenies, B., With Contri.By, Malik, A., With Contri.By, Martinez, J. E. R., With Contri.By, Mills, D. C., With Contri.By, Moeller, T. D., With Contri.By, Palomares, L. A., With Contri.By, Pralow, A., With Contri.By, RamÚrez, O. T., With Contri.By, Rapp, E., With Contri.By, Reichl, U., With Contri.By, Rexer, T., With Contri.By, Sack, M., With Contri.By, Schillberg, S., With Contri.By, Schön, K., With Contri.By, Seeberger, P. H., With Contri.By, Srivastava, I. K., With Contri.By, Stoger, E., With Contri.By, Thomas, B., With Contri.By, Twyman, R. M., With Contri.By, Van Landuyt, L., With Contri.By, Varón Silva, D., With Contri.By, Wang, Q., With Contri.By, Weyant, K. B., With Contri.By, and Yates, L. E., With Contri.By
- Published
- 2021
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17. Correction to: Animal Cell Expression Systems
- Author
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Butler, M., Reichl, U., Scheper, Thomas, Series Editor, Belkin, Shimshon, Editorial Board Member, Bley, Thomas, Editorial Board Member, Bohlmann, Jörg, Editorial Board Member, Gu, Man Bock, Editorial Board Member, Hu, Wei-Shou, Editorial Board Member, Mattiasson, Bo, Editorial Board Member, Olsson, Lisbeth, Editorial Board Member, Seitz, Harald, Editorial Board Member, Silva, Ana Catarina, Editorial Board Member, Ulber, Roland, Editorial Board Member, Zeng, An-Ping, Editorial Board Member, Zhong, Jian-Jiang, Editorial Board Member, Zhou, Weichang, Editorial Board Member, Rapp, Erdmann, editor, Reichl, Udo, editor, Alagesan, K., With Contri.By, Betenbaugh, M. J., With Contri.By, Butler, M., With Contri.By, Buyel, J. F., With Contri.By, Cajic, S., With Contri.By, Callewaert, N., With Contri.By, Can, Ö., With Contri.By, Cox, M. M. J., With Contri.By, DeLisa, M. P., With Contri.By, De Wachter, C., With Contri.By, Elling, L., With Contri.By, Fischer, R., With Contri.By, Flitsch, S. L., With Contri.By, Frohnmeyer, H., With Contri.By, Gottschalk, J., With Contri.By, Goyette-Desjardins, G., With Contri.By, Heffner, K. M., With Contri.By, Hizal, D. B., With Contri.By, Hoffmann, M., With Contri.By, Holland, T., With Contri.By, Jefferis, R., With Contri.By, Kolarich, D., With Contri.By, Laaf, D., With Contri.By, Lepenies, B., With Contri.By, Malik, A., With Contri.By, Martinez, J. E. R., With Contri.By, Mills, D. C., With Contri.By, Moeller, T. D., With Contri.By, Palomares, L. A., With Contri.By, Pralow, A., With Contri.By, RamÚrez, O. T., With Contri.By, Rapp, E., With Contri.By, Reichl, U., With Contri.By, Rexer, T., With Contri.By, Sack, M., With Contri.By, Schillberg, S., With Contri.By, Schön, K., With Contri.By, Seeberger, P. H., With Contri.By, Srivastava, I. K., With Contri.By, Stoger, E., With Contri.By, Thomas, B., With Contri.By, Twyman, R. M., With Contri.By, Van Landuyt, L., With Contri.By, Varón Silva, D., With Contri.By, Wang, Q., With Contri.By, Weyant, K. B., With Contri.By, and Yates, L. E., With Contri.By
- Published
- 2021
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18. Erratum to: Animal Cell Expression Systems
- Author
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Butler, M., Reichl, U., Scheper, Thomas, Series Editor, Belkin, Shimshon, Editorial Board Member, Bley, Thomas, Editorial Board Member, Bohlmann, Jörg, Editorial Board Member, Gu, Man Bock, Editorial Board Member, Hu, Wei-Shou, Editorial Board Member, Mattiasson, Bo, Editorial Board Member, Olsson, Lisbeth, Editorial Board Member, Seitz, Harald, Editorial Board Member, Silva, Ana Catarina, Editorial Board Member, Ulber, Roland, Editorial Board Member, Zeng, An-Ping, Editorial Board Member, Zhong, Jian-Jiang, Editorial Board Member, Zhou, Weichang, Editorial Board Member, Rapp, Erdmann, editor, Reichl, Udo, editor, Alagesan, K., With Contri.By, Betenbaugh, M. J., With Contri.By, Butler, M., With Contri.By, Buyel, J. F., With Contri.By, Cajic, S., With Contri.By, Callewaert, N., With Contri.By, Can, Ö., With Contri.By, Cox, M. M. J., With Contri.By, DeLisa, M. P., With Contri.By, De Wachter, C., With Contri.By, Elling, L., With Contri.By, Fischer, R., With Contri.By, Flitsch, S. L., With Contri.By, Frohnmeyer, H., With Contri.By, Gottschalk, J., With Contri.By, Goyette-Desjardins, G., With Contri.By, Heffner, K. M., With Contri.By, Hizal, D. B., With Contri.By, Hoffmann, M., With Contri.By, Holland, T., With Contri.By, Jefferis, R., With Contri.By, Kolarich, D., With Contri.By, Laaf, D., With Contri.By, Lepenies, B., With Contri.By, Malik, A., With Contri.By, Martinez, J. E. R., With Contri.By, Mills, D. C., With Contri.By, Moeller, T. D., With Contri.By, Palomares, L. A., With Contri.By, Pralow, A., With Contri.By, RamÚrez, O. T., With Contri.By, Rapp, E., With Contri.By, Reichl, U., With Contri.By, Rexer, T., With Contri.By, Sack, M., With Contri.By, Schillberg, S., With Contri.By, Schön, K., With Contri.By, Seeberger, P. H., With Contri.By, Srivastava, I. K., With Contri.By, Stoger, E., With Contri.By, Thomas, B., With Contri.By, Twyman, R. M., With Contri.By, Van Landuyt, L., With Contri.By, Varón Silva, D., With Contri.By, Wang, Q., With Contri.By, Weyant, K. B., With Contri.By, and Yates, L. E., With Contri.By
- Published
- 2021
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19. Correction to: Enzymatic Synthesis of Glycans and Glycoconjugates
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Rexer, Thomas, Laaf, Dominic, Gottschalk, Johannes, Frohnmeyer, Hannes, Rapp, Erdmann, Elling, Lothar, Scheper, Thomas, Series Editor, Belkin, Shimshon, Editorial Board Member, Bley, Thomas, Editorial Board Member, Bohlmann, Jörg, Editorial Board Member, Gu, Man Bock, Editorial Board Member, Hu, Wei-Shou, Editorial Board Member, Mattiasson, Bo, Editorial Board Member, Olsson, Lisbeth, Editorial Board Member, Seitz, Harald, Editorial Board Member, Silva, Ana Catarina, Editorial Board Member, Ulber, Roland, Editorial Board Member, Zeng, An-Ping, Editorial Board Member, Zhong, Jian-Jiang, Editorial Board Member, Zhou, Weichang, Editorial Board Member, Rapp, Erdmann, editor, Reichl, Udo, editor, Alagesan, K., With Contri.By, Betenbaugh, M. J., With Contri.By, Butler, M., With Contri.By, Buyel, J. F., With Contri.By, Cajic, S., With Contri.By, Callewaert, N., With Contri.By, Can, Ö., With Contri.By, Cox, M. M. J., With Contri.By, DeLisa, M. P., With Contri.By, De Wachter, C., With Contri.By, Elling, L., With Contri.By, Fischer, R., With Contri.By, Flitsch, S. L., With Contri.By, Frohnmeyer, H., With Contri.By, Gottschalk, J., With Contri.By, Goyette-Desjardins, G., With Contri.By, Heffner, K. M., With Contri.By, Hizal, D. B., With Contri.By, Hoffmann, M., With Contri.By, Holland, T., With Contri.By, Jefferis, R., With Contri.By, Kolarich, D., With Contri.By, Laaf, D., With Contri.By, Lepenies, B., With Contri.By, Malik, A., With Contri.By, Martinez, J. E. R., With Contri.By, Mills, D. C., With Contri.By, Moeller, T. D., With Contri.By, Palomares, L. A., With Contri.By, Pralow, A., With Contri.By, RamÚrez, O. T., With Contri.By, Rapp, E., With Contri.By, Reichl, U., With Contri.By, Rexer, T., With Contri.By, Sack, M., With Contri.By, Schillberg, S., With Contri.By, Schön, K., With Contri.By, Seeberger, P. H., With Contri.By, Srivastava, I. K., With Contri.By, Stoger, E., With Contri.By, Thomas, B., With Contri.By, Twyman, R. M., With Contri.By, Van Landuyt, L., With Contri.By, Varón Silva, D., With Contri.By, Wang, Q., With Contri.By, Weyant, K. B., With Contri.By, and Yates, L. E., With Contri.By
- Published
- 2021
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20. Macrophage- and CD4+ T cell-derived SIV differ in glycosylation, infectivity and neutralization sensitivity.
- Author
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Karsten CB, Buettner FFR, Cajic S, Nehlmeier I, Roshani B, Klippert A, Sauermann U, Stolte-Leeb N, Reichl U, Gerardy-Schahn R, Rapp E, Stahl-Hennig C, and Pöhlmann S
- Subjects
- Glycosylation, Animals, Humans, Macaca mulatta, Polysaccharides metabolism, Polysaccharides immunology, Simian Immunodeficiency Virus immunology, CD4-Positive T-Lymphocytes immunology, CD4-Positive T-Lymphocytes virology, Macrophages virology, Macrophages immunology, Macrophages metabolism, Antibodies, Neutralizing immunology, Simian Acquired Immunodeficiency Syndrome immunology, Simian Acquired Immunodeficiency Syndrome virology, Simian Acquired Immunodeficiency Syndrome metabolism
- Abstract
The human immunodeficiency virus (HIV) envelope protein (Env) mediates viral entry into host cells and is the primary target for the humoral immune response. Env is extensively glycosylated, and these glycans shield underlying epitopes from neutralizing antibodies. The glycosylation of Env is influenced by the type of host cell in which the virus is produced. Thus, HIV is distinctly glycosylated by CD4+ T cells, the major target cells, and macrophages. However, the specific differences in glycosylation between viruses produced in these cell types have not been explored at the molecular level. Moreover, it remains unclear whether the production of HIV in CD4+ T cells or macrophages affects the efficiency of viral spread and resistance to neutralization. To address these questions, we employed the simian immunodeficiency virus (SIV) model. Glycan analysis implied higher relative levels of oligomannose-type N-glycans in SIV from CD4+ T cells (T-SIV) compared to SIV from macrophages (M-SIV), and the complex-type N-glycans profiles seem to differ between the two viruses. Notably, M-SIV demonstrated greater infectivity than T-SIV, even when accounting for Env incorporation, suggesting that host cell-dependent factors influence infectivity. Further, M-SIV was more efficiently disseminated by HIV binding cellular lectins. We also evaluated the influence of cell type-dependent differences on SIV's vulnerability to carbohydrate binding agents (CBAs) and neutralizing antibodies. T-SIV demonstrated greater susceptibility to mannose-specific CBAs, possibly due to its elevated expression of oligomannose-type N-glycans. In contrast, M-SIV exhibited higher susceptibility to neutralizing sera in comparison to T-SIV. These findings underscore the importance of host cell-dependent attributes of SIV, such as glycosylation, in shaping both infectivity and the potential effectiveness of intervention strategies., Competing Interests: The authors have declared that no competing interests exist., (Copyright: © 2024 Karsten et al. This is an open access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.)
- Published
- 2024
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21. Genetic knockout of porcine GGTA1 or CMAH/GGTA1 is associated with the emergence of neo-glycans.
- Author
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Morticelli L, Rossdam C, Cajic S, Böthig D, Magdei M, Tuladhar SR, Petersen B, Fischer K, Rapp E, Korossis S, Haverich A, Schnieke A, Niemann H, Buettner FFR, and Hilfiker A
- Subjects
- Animals, Swine, Humans, Animals, Genetically Modified, Transplantation, Heterologous methods, Gene Knockout Techniques, Epitopes, Galactosyltransferases genetics, Polysaccharides
- Abstract
Background: Pig-derived tissues could overcome the shortage of human donor organs in transplantation. However, the glycans with terminal α-Gal and Neu5Gc, which are synthesized by enzymes, encoded by the genes GGTA1 and CMAH, are known to play a major role in immunogenicity of porcine tissue, ultimately leading to xenograft rejection., Methods: The N-glycome and glycosphingolipidome of native and decellularized porcine pericardia from wildtype (WT), GGTA1-KO and GGTA1/CMAH-KO pigs were analyzed by multiplexed capillary gel electrophoresis coupled to laser-induced fluorescence detection., Results: We identified biantennary and core-fucosylated N-glycans terminating with immunogenic α-Gal- and α-Gal-/Neu5Gc-epitopes on pericardium of WT pigs that were absent in GGTA1 and GGTA1/CMAH-KO pigs, respectively. Levels of N-glycans terminating with galactose bound in β(1-4)-linkage to N-acetylglucosamine and their derivatives elongated by Neu5Ac were increased in both KO groups. N-glycans capped with Neu5Gc were increased in GGTA1-KO pigs compared to WT, but were not detected in GGTA1/CMAH-KO pigs. Similarly, the ganglioside Neu5Gc-GM3 was found in WT and GGTA1-KO but not in GGTA1/CMAH-KO pigs. The applied detergent based decellularization efficiently removed GSL glycans., Conclusion: Genetic deletion of GGTA1 or GGTA1/CMAH removes specific epitopes providing a more human-like glycosylation pattern, but at the same time changes distribution and levels of other porcine glycans that are potentially immunogenic., (© 2023 The Authors. Xenotransplantation published by John Wiley & Sons Ltd.)
- Published
- 2023
- Full Text
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22. Reliable N -Glycan Analysis-Removal of Frequently Occurring Oligosaccharide Impurities by Enzymatic Degradation.
- Author
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Burock R, Cajic S, Hennig R, Buettner FFR, Reichl U, and Rapp E
- Subjects
- Glycosylation, Polysaccharides chemistry, Protein Processing, Post-Translational, Glycoproteins chemistry, Oligosaccharides metabolism
- Abstract
Glycosylation, especially N -glycosylation, is one of the most common protein modifications, with immense importance at the molecular, cellular, and organismal level. Thus, accurate and reliable N -glycan analysis is essential in many areas of pharmaceutical and food industry, medicine, and science. However, due to the complexity of the cellular glycosylation process, in-depth glycoanalysis is still a highly challenging endeavor. Contamination of samples with oligosaccharide impurities (OSIs), typically linear glucose homo-oligomers, can cause further complications. Due to their physicochemical similarity to N -glycans, OSIs produce potentially overlapping signals, which can remain unnoticed. If recognized, suspected OSI signals are usually excluded in data evaluation. However, in both cases, interpretation of results can be impaired. Alternatively, sample preparation can be repeated to include an OSI removal step from samples. However, this significantly increases sample amount, time, and effort necessary. To overcome these issues, we investigated the option to enzymatically degrade and thereby remove interfering OSIs as a final sample preparation step. Therefore, we screened ten commercially available enzymes concerning their potential to efficiently degrade maltodextrins and dextrans as most frequently found OSIs. Of these enzymes, only dextranase from Chaetomium erraticum and glucoamylase P from Hormoconis resinae enabled a degradation of OSIs within only 30 min that is free of side reactions with N -glycans. Finally, we applied the straightforward enzymatic degradation of OSIs to N -glycan samples derived from different standard glycoproteins and various stem cell lysates.
- Published
- 2023
- Full Text
- View/download PDF
23. Combining functional metagenomics and glycoanalytics to identify enzymes that facilitate structural characterization of sulfated N-glycans.
- Author
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Chuzel L, Fossa SL, Boisvert ML, Cajic S, Hennig R, Ganatra MB, Reichl U, Rapp E, and Taron CH
- Subjects
- Enzymes genetics, Kinetics, Sulfates chemistry, Acetylglucosamine metabolism, Enzymes isolation & purification, Enzymes metabolism, Metagenomics methods, Polysaccharides chemistry, Polysaccharides metabolism, Sulfates metabolism
- Abstract
Background: Sulfate modification of N-glycans is important for several biological functions such as clearance of pituitary hormones or immunoregulation. Yet, the prevalence of this N-glycan modification and its functions remain largely unexplored. Characterization of N-glycans bearing sulfate modifications is hampered in part by a lack of enzymes that enable site-specific detection of N-glycan sulfation. In this study, we used functional metagenomic screening to identify enzymes that act upon sulfated N-acetylglucosamine (GlcNAc). Using multiplexed capillary gel electrophoresis with laser-induced fluorescence detection (xCGE-LIF) -based glycoanalysis we proved their ability to act upon GlcNAc-6-SO
4 on N-glycans., Results: Our screen identified a sugar-specific sulfatase that specifically removes sulfate from GlcNAc-6-SO4 when it is in a terminal position on an N-glycan. Additionally, in the absence of calcium, this sulfatase binds to the sulfated glycan but does not remove the sulfate group, suggesting it could be used for selective isolation of sulfated N-glycans. Further, we describe isolation of a sulfate-dependent hexosaminidase that removes intact GlcNAc-6-SO4 (but not asulfated GlcNAc) from a terminal position on N-glycans. Finally, the use of these enzymes to detect the presence of sulfated N-glycans by xCGE-LIF is demonstrated., Conclusion: The present study demonstrates the feasibility of using functional metagenomic screening combined with glycoanalytics to discover enzymes that act upon chemical modifications of glycans. The discovered enzymes represent new specificities that can help resolve the presence of GlcNAc-6-SO4 in N-glycan structural analyses., (© 2021. The Author(s).)- Published
- 2021
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24. Capillary (Gel) Electrophoresis-Based Methods for Immunoglobulin (G) Glycosylation Analysis.
- Author
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Cajic S, Hennig R, Burock R, and Rapp E
- Subjects
- Antibodies, Monoclonal, Glycosylation, Humans, Mass Spectrometry, Electrophoresis, Capillary, Immunoglobulin G
- Abstract
The in-depth characterization of protein glycosylation has become indispensable in many research fields and in the biopharmaceutical industry. Especially knowledge about modulations in immunoglobulin G (IgG) N-glycosylation and their effect on immunity enabled a better understanding of human diseases and the development of new, more effective drugs for their treatment. This chapter provides a deeper insight into capillary (gel) electrophoresis-based (C(G)E) glycan analysis, addressing its impressive performance and possibilities, its great potential regarding real high-throughput for large cohort studies, as well as its challenges and limitations. We focus on the latest developments with respect to miniaturization and mass spectrometry coupling, as well as data analysis and interpretation. The use of exoglycosidase sequencing in combination with current C(G)E technology is discussed, highlighting possible difficulties and pitfalls. The application section describes the detailed characterization of N-glycosylation, utilizing multiplexed CGE with laser-induced fluorescence detection (xCGE-LIF). Besides a comprehensive overview on antibody glycosylation by comparing species-specific IgGs and human immunoglobulins A, D, E, G, and M, the chapter comprises a comparison of therapeutic monoclonal antibodies from different production cell lines, as well as a detailed characterization of Fab and Fc glycosylation. These examples illustrate the full potential of C(G)E, resolving the smallest differences in sugar composition and structure., (© 2021. The Author(s).)
- Published
- 2021
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25. NIST Interlaboratory Study on Glycosylation Analysis of Monoclonal Antibodies: Comparison of Results from Diverse Analytical Methods.
- Author
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De Leoz MLA, Duewer DL, Fung A, Liu L, Yau HK, Potter O, Staples GO, Furuki K, Frenkel R, Hu Y, Sosic Z, Zhang P, Altmann F, Grunwald-Grube C, Shao C, Zaia J, Evers W, Pengelley S, Suckau D, Wiechmann A, Resemann A, Jabs W, Beck A, Froehlich JW, Huang C, Li Y, Liu Y, Sun S, Wang Y, Seo Y, An HJ, Reichardt NC, Ruiz JE, Archer-Hartmann S, Azadi P, Bell L, Lakos Z, An Y, Cipollo JF, Pucic-Bakovic M, Štambuk J, Lauc G, Li X, Wang PG, Bock A, Hennig R, Rapp E, Creskey M, Cyr TD, Nakano M, Sugiyama T, Leung PA, Link-Lenczowski P, Jaworek J, Yang S, Zhang H, Kelly T, Klapoetke S, Cao R, Kim JY, Lee HK, Lee JY, Yoo JS, Kim SR, Suh SK, de Haan N, Falck D, Lageveen-Kammeijer GSM, Wuhrer M, Emery RJ, Kozak RP, Liew LP, Royle L, Urbanowicz PA, Packer NH, Song X, Everest-Dass A, Lattová E, Cajic S, Alagesan K, Kolarich D, Kasali T, Lindo V, Chen Y, Goswami K, Gau B, Amunugama R, Jones R, Stroop CJM, Kato K, Yagi H, Kondo S, Yuen CT, Harazono A, Shi X, Magnelli PE, Kasper BT, Mahal L, Harvey DJ, O'Flaherty R, Rudd PM, Saldova R, Hecht ES, Muddiman DC, Kang J, Bhoskar P, Menard D, Saati A, Merle C, Mast S, Tep S, Truong J, Nishikaze T, Sekiya S, Shafer A, Funaoka S, Toyoda M, de Vreugd P, Caron C, Pradhan P, Tan NC, Mechref Y, Patil S, Rohrer JS, Chakrabarti R, Dadke D, Lahori M, Zou C, Cairo C, Reiz B, Whittal RM, Lebrilla CB, Wu L, Guttman A, Szigeti M, Kremkow BG, Lee KH, Sihlbom C, Adamczyk B, Jin C, Karlsson NG, Örnros J, Larson G, Nilsson J, Meyer B, Wiegandt A, Komatsu E, Perreault H, Bodnar ED, Said N, Francois YN, Leize-Wagner E, Maier S, Zeck A, Heck AJR, Yang Y, Haselberg R, Yu YQ, Alley W, Leone JW, Yuan H, and Stein SE
- Subjects
- Antibodies, Monoclonal metabolism, Glycomics methods, Glycopeptides metabolism, Glycosylation, Humans, Laboratories, Polysaccharides metabolism, Protein Processing, Post-Translational, Proteomics methods, Antibodies, Monoclonal chemistry, Biological Products, Biopharmaceutics methods
- Abstract
Glycosylation is a topic of intense current interest in the development of biopharmaceuticals because it is related to drug safety and efficacy. This work describes results of an interlaboratory study on the glycosylation of the Primary Sample (PS) of NISTmAb, a monoclonal antibody reference material. Seventy-six laboratories from industry, university, research, government, and hospital sectors in Europe, North America, Asia, and Australia submitted a total of 103 reports on glycan distributions. The principal objective of this study was to report and compare results for the full range of analytical methods presently used in the glycosylation analysis of mAbs. Therefore, participation was unrestricted, with laboratories choosing their own measurement techniques. Protein glycosylation was determined in various ways, including at the level of intact mAb, protein fragments, glycopeptides, or released glycans, using a wide variety of methods for derivatization, separation, identification, and quantification. Consequently, the diversity of results was enormous, with the number of glycan compositions identified by each laboratory ranging from 4 to 48. In total, one hundred sixteen glycan compositions were reported, of which 57 compositions could be assigned consensus abundance values. These consensus medians provide community-derived values for NISTmAb PS. Agreement with the consensus medians did not depend on the specific method or laboratory type. The study provides a view of the current state-of-the-art for biologic glycosylation measurement and suggests a clear need for harmonization of glycosylation analysis methods., (© 2020 De Leoz et al.)
- Published
- 2020
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26. Enzymatic Cascades for Tailored 13 C 6 and 15 N Enriched Human Milk Oligosaccharides.
- Author
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Fischöder T, Cajic S, Grote V, Heinzler R, Reichl U, Franzreb M, Rapp E, and Elling L
- Subjects
- Carbon Isotopes chemistry, Catalysis, Glycosyltransferases chemistry, Humans, Nitrogen Isotopes chemistry, Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization, Uracil Nucleotides chemistry, Milk, Human chemistry, Oligosaccharides chemistry
- Abstract
Several health benefits, associated with human milk oligosaccharides (HMOS), have been revealed in the last decades. Further progress, however, requires not only the establishment of a simple "routine" method for absolute quantification of complex HMOS mixtures but also the development of novel synthesis strategies to improve access to tailored HMOS. Here, we introduce a combination of salvage-like nucleotide sugar-producing enzyme cascades with Leloir -glycosyltransferases in a sequential pattern for the convenient tailoring of stable isotope-labeled HMOS. We demonstrate the assembly of [
13 C6 ]galactose into lacto- N - and lacto- N -neo-type HMOS structures up to octaoses. Further, we present the enzymatic production of UDP-[15 N]GlcNAc and its application for the enzymatic synthesis of [13 C6 /15 N]lacto- N -neo-tetraose for the first time. An exemplary application was selected-analysis of tetraose in complex biological mixtures-to show the potential of tailored stable isotope reference standards for the mass spectrometry-based quantification, using matrix-assisted laser desorption/ionization-time of flight mass spectrometry (MALDI-TOF-MS) as a fast and straightforward method for absolute quantification of HMOS. Together with the newly available well-defined tailored isotopic HMOS, this can make a crucial contribution to prospective research aiming for a more profound understanding of HMOS structure-function relations., Competing Interests: The authors declare no conflicts of interest.- Published
- 2019
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27. Enzymatic Cascade Synthesis Provides Novel Linear Human Milk Oligosaccharides as Reference Standards for xCGE-LIF Based High-Throughput Analysis.
- Author
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Fischöder T, Cajic S, Reichl U, Rapp E, and Elling L
- Subjects
- Electrophoresis, Capillary methods, Fluorescence, Humans, Lasers, Protein Biosynthesis physiology, Recombinant Fusion Proteins metabolism, Reference Standards, Glycosyltransferases metabolism, Milk, Human metabolism, Oligosaccharides metabolism
- Abstract
A rising amount of known health benefits leads to an increased attention of science and nutrient industry to human milk oligosaccharides (HMOS). The unique diversity of HMOS includes several rare, complex, and high molecular weight structures. Therefore, identification and elucidation of complex structures, which may occur only in traces, poses a daunting analytical challenge, further complicated by the limited access to suitable standards. Regarding this, inherent diversity of HMOS and their structural complexity make them difficult to synthesize. The use of recombinant Leloir-glycosyltransferases offers a common strategy to overcome the latter issues. In this study, linear long-chained Lacto-N-biose-type (LNT) and Lacto-N-neo-type (LNnT) HMOS are tailored far beyond the known naturally occurring length. Thereby novel well-defined reference standards for screening HMOS composition by high performance and high throughput analytics are provided. It is shown here for the first time the synthesis of LNT oligomers up to 26 and LNnT oligomers up to 30 sugar units in a semi-sequential one-pot synthesis as analyzed by high performance multiplexed capillary gel electrophoresis with laser-induced fluorescence detection (xCGE-LIF). While being a high-throughput method, xCGE-LIF can also handle long chained linkage isomers of challenging similarity, some of them even present only in trace amounts., (© 2018 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.)
- Published
- 2019
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- View/download PDF
28. Quantitative Assessment of Sialo-Glycoproteins and N-Glycans during Cardiomyogenic Differentiation of Human Induced Pluripotent Stem Cells.
- Author
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Konze SA, Cajic S, Oberbeck A, Hennig R, Pich A, Rapp E, and Buettner FFR
- Subjects
- Acetylglucosamine chemistry, Acetylglucosamine metabolism, Carbohydrate Sequence, Cell Differentiation, Cell Membrane metabolism, Ciliary Neurotrophic Factor Receptor alpha Subunit genetics, Ciliary Neurotrophic Factor Receptor alpha Subunit metabolism, Fucose chemistry, Fucose metabolism, Galactose chemistry, Galactose metabolism, Gastrins genetics, Gastrins metabolism, Gene Expression Regulation, Humans, Induced Pluripotent Stem Cells cytology, Induced Pluripotent Stem Cells metabolism, Laminin genetics, Laminin metabolism, Membrane Proteins genetics, Membrane Proteins metabolism, Myocytes, Cardiac cytology, Myocytes, Cardiac metabolism, Polysaccharides metabolism, Receptor, EphA7 genetics, Receptor, EphA7 metabolism, Receptor-Like Protein Tyrosine Phosphatases, Class 2 genetics, Receptor-Like Protein Tyrosine Phosphatases, Class 2 metabolism, Receptors, G-Protein-Coupled genetics, Receptors, G-Protein-Coupled metabolism, Sialic Acids chemistry, Sialic Acids metabolism, Staining and Labeling methods, Cell Membrane chemistry, Glycomics methods, Induced Pluripotent Stem Cells chemistry, Myocytes, Cardiac chemistry, Polysaccharides chemistry
- Abstract
Human induced pluripotent stem-cell-derived cardiomyocytes (hiPSC CMs) may be used in regenerative medicine for individualized tissue transplants in the future. For application in patients, the generated CMs have to be highly pure and well characterized. In order to overcome the prevalent scarcity of CM-specific markers, we quantitatively assessed cell-surface-exposed sialo-glycoproteins and N-glycans of hiPSCs, CM progenitors, and CMs. Applying a combination of metabolic labeling and specific sialo-glycoprotein capture, we could highly enrich and quantify membrane proteins during cardiomyogenic differentiation. Among them we identified a number of novel, putative biomarkers for hiPSC CMs. Analysis of the N-glycome by capillary gel electrophoresis revealed three novel structures comprising β1,3-linked galactose, α2,6-linked sialic acid and complex fucosylation; these were highly specific for hiPSCs. Bisecting GlcNAc structures strongly increased during differentiation, and we propose that they are characteristic of early, immature CMs., (© 2017 Wiley-VCH Verlag GmbH & Co. KGaA, Weinheim.)
- Published
- 2017
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29. Sialylation Is Dispensable for Early Murine Embryonic Development in Vitro.
- Author
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Abeln M, Borst KM, Cajic S, Thiesler H, Kats E, Albers I, Kuhn M, Kaever V, Rapp E, Münster-Kühnel A, and Weinhold B
- Subjects
- Amino Sugars metabolism, Animals, Cell Differentiation, Cell Line, Embryo, Mammalian, Embryoid Bodies cytology, Embryoid Bodies metabolism, Founder Effect, Galactose metabolism, Gene Expression, Germ Layers cytology, Glycoconjugates metabolism, HEK293 Cells, Humans, Mice, Mice, Inbred C57BL, Mice, Transgenic, Mouse Embryonic Stem Cells cytology, Myocytes, Cardiac cytology, N-Acylneuraminate Cytidylyltransferase genetics, Pluripotent Stem Cells cytology, Transcriptome, Germ Layers metabolism, Mouse Embryonic Stem Cells metabolism, Myocytes, Cardiac metabolism, N-Acylneuraminate Cytidylyltransferase deficiency, Pluripotent Stem Cells metabolism, Sialic Acids metabolism
- Abstract
The negatively charged nonulose sialic acid (Sia) is essential for murine development in vivo. In order to elucidate the impact of sialylation on differentiation processes in the absence of maternal influences, we generated mouse embryonic stem cell (mESC) lines that lack CMP-Sia synthetase (CMAS) and thereby the ability to activate Sia to CMP-Sia. Loss of CMAS activity resulted in an asialo cell surface accompanied by an increase in glycoconjugates with terminal galactosyl and oligo-LacNAc residues, as well as intracellular accumulation of free Sia. Remarkably, these changes did not impact intracellular metabolites or the morphology and transcriptome of pluripotent mESC lines. Moreover, the capacity of Cmas
-/- mESCs for undirected differentiation into embryoid bodies, germ layer formation and even the generation of beating cardiomyocytes provides first and conclusive evidence that pluripotency and differentiation of mESC in vitro can proceed in the absence of (poly)sialoglycans., (© 2017 The Authors. Published by Wiley-VCH Verlag GmbH & Co. KGaA.)- Published
- 2017
- Full Text
- View/download PDF
30. Towards personalized diagnostics via longitudinal study of the human plasma N-glycome.
- Author
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Hennig R, Cajic S, Borowiak M, Hoffmann M, Kottler R, Reichl U, and Rapp E
- Subjects
- Adult, Follow-Up Studies, Humans, Male, Glycomics methods, Polysaccharides blood, Precision Medicine
- Abstract
Facilitated by substantial advances in analytical methods, plasma N-glycans have emerged as potential candidates for biomarkers. In the recent years, several investigations could link aberrant plasma N-glycosylation to numerous diseases. However, due to often limited specificity and sensitivity, only a very limited number of glycan biomarkers were approved by the authorities up to now. The inter-individual heterogeneity of the plasma N-glycomes might mask disease related changes in conventional large cross-sectional cohort studies, with a one-time sampling approach. But, a possible benefit of longitudinal sampling in biomarker discovery could be, that already small changes during disease progression are revealed, by monitoring the plasma N-glycome of individuals over time. To evaluate this, we collected blood plasma samples of five healthy donors over a time period of up to six years (min. 1.5 years). The plasma N-glycome was analyzed by xCGE-LIF, to investigate the intra-individual N-glycome variability over time. It is shown, that the plasma N-glycome of an individual is remarkably stable over a period of several years, and that observed small longitudinal changes are independent from seasons, but significantly correlated with lifestyle and environmental factors. Thus, the potential of future longitudinal biomarker discovery studies could be demonstrated, which is a further step towards personalized diagnostics. This article is part of a Special Issue entitled "Glycans in personalised medicine" Guest Editor: Professor Gordan Lauc., (Copyright © 2016 The Authors. Published by Elsevier B.V. All rights reserved.)
- Published
- 2016
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31. Glycomic Characterization of Induced Pluripotent Stem Cells Derived from a Patient Suffering from Phosphomannomutase 2 Congenital Disorder of Glycosylation (PMM2-CDG).
- Author
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Thiesler CT, Cajic S, Hoffmann D, Thiel C, van Diepen L, Hennig R, Sgodda M, Weiβmann R, Reichl U, Steinemann D, Diekmann U, Huber NM, Oberbeck A, Cantz T, Kuss AW, Körner C, Schambach A, Rapp E, and Buettner FF
- Subjects
- Cells, Cultured, Congenital Disorders of Glycosylation metabolism, Gene Expression Profiling methods, Glycosylation, High-Throughput Nucleotide Sequencing methods, Humans, Induced Pluripotent Stem Cells pathology, Phosphotransferases (Phosphomutases) metabolism, Polysaccharides metabolism, Congenital Disorders of Glycosylation pathology, Glycomics methods, Induced Pluripotent Stem Cells metabolism, Models, Biological, Phosphotransferases (Phosphomutases) deficiency
- Abstract
PMM2-CDG, formerly known as congenital disorder of glycosylation-Ia (CDG-Ia), is caused by mutations in the gene encoding phosphomannomutase 2 (PMM2). This disease is the most frequent form of inherited CDG-diseases affecting protein N-glycosylation in human. PMM2-CDG is a multisystemic disease with severe psychomotor and mental retardation. In order to study the pathophysiology of PMM2-CDG in a human cell culture model, we generated induced pluripotent stem cells (iPSCs) from fibroblasts of a PMM2-CDG-patient (PMM2-iPSCs). Expression of pluripotency factors andin vitrodifferentiation into cell types of the three germ layers was unaffected in the analyzed clone PMM2-iPSC-C3 compared with nondiseased human pluripotent stem cells (hPSCs), revealing no broader influence of the PMM2 mutation on pluripotency in cell culture. Analysis of gene expression by deep-sequencing did not show obvious differences in the transcriptome between PMM2-iPSC-C3 and nondiseased hPSCs. By multiplexed capillary gel electrophoresis coupled to laser induced fluorescence detection (xCGE-LIF) we could show that PMM2-iPSC-C3 exhibit the common hPSC N-glycosylation pattern with high-mannose-type N-glycans as the predominant species. However, phosphomannomutase activity of PMM2-iPSC-C3 was 27% compared with control hPSCs and lectin staining revealed an overall reduced protein glycosylation. In addition, quantitative assessment of N-glycosylation by xCGE-LIF showed an up to 40% reduction of high-mannose-type N-glycans in PMM2-iPSC-C3, which was in concordance to the observed reduction of the Glc3Man9GlcNAc2 lipid-linked oligosaccharide compared with control hPSCs. Thus we could model the PMM2-CDG disease phenotype of hypoglycosylation with patient derived iPSCsin vitro Knock-down ofPMM2by shRNA in PMM2-iPSC-C3 led to a residual activity of 5% and to a further reduction of the level of N-glycosylation. Taken together we have developed human stem cell-based cell culture models with stepwise reduced levels of N-glycosylation now enabling to study the role of N-glycosylation during early human development., (© 2016 by The American Society for Biochemistry and Molecular Biology, Inc.)
- Published
- 2016
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32. Exclusive Decoration of Simian Immunodeficiency Virus Env with High-Mannose Type N-Glycans Is Not Compatible with Mucosal Transmission in Rhesus Macaques.
- Author
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Karsten CB, Buettner FF, Cajic S, Nehlmeier I, Neumann B, Klippert A, Sauermann U, Reichl U, Gerardy-Schahn R, Rapp E, Stahl-Hennig C, and Pöhlmann S
- Subjects
- Animals, Cell Line, HIV Infections transmission, HIV Infections virology, HIV-1 metabolism, HIV-1 pathogenicity, Humans, Macaca mulatta, Mannose metabolism, Simian Acquired Immunodeficiency Syndrome virology, Simian Immunodeficiency Virus metabolism, Gene Products, env metabolism, Mucous Membrane virology, Polysaccharides metabolism, Simian Acquired Immunodeficiency Syndrome transmission, Simian Immunodeficiency Virus pathogenicity
- Abstract
Human immunodeficiency virus (HIV) and simian immunodeficiency virus (SIV) envelope (Env) proteins are extensively decorated with N-glycans, predominantly of the high-mannose type. However, it is unclear how high-mannose N-glycans on Env impact viral spread. We show that exclusive modification of SIV Env with these N-glycans reduces viral infectivity and abrogates mucosal transmission, despite increasing viral capture by immune cell lectins. Thus, high-mannose N-glycans have opposed effects on SIV infectivity and lectin reactivity, and a balance might be required for efficient mucosal transmission., (Copyright © 2015, Karsten et al.)
- Published
- 2015
- Full Text
- View/download PDF
33. N-Glycosylation Fingerprinting of Viral Glycoproteins by xCGE-LIF.
- Author
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Hennig R, Rapp E, Kottler R, Cajic S, Borowiak M, and Reichl U
- Subjects
- Animals, Antigens, Viral immunology, Cell Culture Techniques, Dogs, Electrophoresis, Capillary methods, Glycoproteins immunology, Glycosylation, Hemagglutinins chemistry, Hemagglutinins immunology, Influenza A virus immunology, Influenza B virus immunology, Influenza Vaccines immunology, Madin Darby Canine Kidney Cells, Membrane Glycoproteins immunology, Neuraminidase chemistry, Neuraminidase immunology, Polysaccharides chemistry, Polysaccharides immunology, Antigens, Viral chemistry, Glycoproteins chemistry, Membrane Glycoproteins chemistry, Viral Proteins chemistry
- Abstract
The ongoing threat of pathogens, increasing resistance against antibiotics, and the risk of fast spreading of infectious diseases in a global community resulted in an intensified development of vaccines. Antigens used for vaccination comprise a wide variety of macromolecules including glycoproteins, lipopolysaccharides, and complex carbohydrates. For all of these antigens the sugar composition plays a crucial role for immunogenicity and protective efficacy of the vaccine. Here, we provide a protocol for N-glycosylation fingerprinting utilizing high performance multiplexed capillary gel electrophoresis with laser-induced fluorescence detection (xCGE-LIF) technology. The method described, enables to analyze the N-glycosylation of specific proteins out of a complex sample or even the total of all N-glycans contained in such a sample. The protocol is exemplarily demonstrated for N-glycosylation fingerprinting of cell culture-derived influenza A and B viruses and their major antigens, the membrane glycoproteins hemagglutinin and neuraminidase.
- Published
- 2015
- Full Text
- View/download PDF
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