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1. Improved spot morphology for printed glycan arrays

Author

Navakouski Maksim, Shilova Nadezhda, Khasbiullina Nailya, Feofanov Alexey, Pudova Elena, Chen Kowa, Blixt Ola, and Bovin Nicolai

Subjects
printed glycan array, spots morphology, glycans, microarray, lab-on-chip, Biology (General), QH301-705.5
Abstract

Despite considerable success studying glycan-binding proteins using printed glycan arrays (PGAs), unambiguous quantitation of spot intensities by fluorescent readers remains a challenge. The main obstacles are the varying spot shape and size and in-spot fluorescence distribution caused by uneven drying of the printed drops. Two methods have been suggested for solving this problem: using polymeric glycoconjugates, which makes it possible to equalize the physicochemical properties (hydrophobicity, charge, and size) of different glycans, and applying a glycan solution on a slide coated with a thin oil mask, which hinders evaporation of the drop. Both approaches yield spots with similar sizes and an even distribution of the signal across the spot and are likely to be useful for improving the prints of other classes of molecules.

Published
2018
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3. Allergic reactions to tick saliva components in zebrafish model

Author

Contreras, Marinela, Vaz-Rodrigues, Rita, Mazuecos, Lorena, Villar, Margarita, Artigas-Jerónimo, Sara, González-García, Almudena, Shilova, Nadezhda V., Bovin, Nicolai V., Díaz-Sánchez, Sandra, Ferreras-Colino, Elisa, Pacheco, Iván, Chmelař, Jindřich, Kopáček, Petr, Cabezas-Cruz, Alejandro, Gortázar, Christian, and de la Fuente, José

Published
2023
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5. 6-sulfo sialyl Lewis X is the common receptor determinant recognized by H5, H6, H7 and H9 influenza viruses of terrestrial poultry

Author

Bovin Nicolai V, Desheva Julia A, Pazynina Galina V, Tuzikov Alexander B, Gambaryan Alexandra S, Matrosovich Mikhail N, and Klimov Alexander I

Subjects
Infectious and parasitic diseases, RC109-216
Abstract

Abstract Background Influenza A viruses of domestic birds originate from the natural reservoir in aquatic birds as a result of interspecies transmission and adaptation to new host species. We previously noticed that influenza viruses isolated from distinct orders of aquatic and terrestrial birds may differ in their fine receptor-binding specificity by recognizing the structure of the inner parts of Neu5Acα2-3Gal-terminated sialyloligosaccharide receptors. To further characterize these differences, we studied receptor-binding properties of a large panel of influenza A viruses from wild aquatic birds, poultry, pigs and horses. Results Using a competitive solid-phase binding assay, we determined viral binding to polymeric conjugates of sialyloligosaccharides differing by the type of Neu5Acα-Gal linkage and by the structure of the more distant parts of the oligosaccharide chain. Influenza viruses isolated from terrestrial poultry differed from duck viruses by an enhanced binding to sulfated and/or fucosylated Neu5Acα2-3Gal-containing sialyloligosaccharides. Most of the poultry viruses tested shared a high binding affinity for the 6-sulfo sialyl Lewis X (Su-SLex). Efficient binding of poultry viruses to Su-SLex was often accompanied by their ability to bind to Neu5Acα2-6Gal-terminated (human-type) receptors. Such a dual receptor-binding specificity was demonstrated for the North American and Eurasian H7 viruses, H9N2 Eurasian poultry viruses, and H1, H3 and H9 avian-like virus isolates from pigs. Conclusion Influenza viruses of terrestrial poultry differ from ancestral duck viruses by enhanced binding to sulfated and/or fucosylated Neu5Acα2-3Gal-terminated receptors and, occasionally, by the ability to bind to Neu5Acα2-6Gal-terminated (human-type) receptors. These findings suggest that the adaptation to receptors in poultry can enhance the potential of an avian virus for avian-to-human transmission and pandemic spread.

Published
2008
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16. A novel syphilis Treponema pallidum lipoprotein peptide antigen diagnostic assay using red cell kodecytes in routine blood centre column agglutination testing platforms.

Author

Datta, Suvro Sankha, Nagappan, Radhika, Biswas, Durba, Basu, Debapriya, Gupta, Kaushik, Mondal, Pradip Kumar, Tuzikov, Alexander, Bovin, Nicolai V., and Henry, Stephen M.

Subjects
TREPONEMA pallidum, ERYTHROCYTES, PEPTIDES, AGGLUTINATION tests, COMMUNICABLE diseases, SYPHILIS
Abstract

Background and Objectives: The detection of treponemal antibodies, which are used to make a diagnosis of syphilis, is important both for diagnostic purposes and as a mandatory blood donor test in most countries. We evaluated the feasibility of using Kode Technology to make syphilis peptide red cell kodecytes for use in column agglutination serologic platforms. Materials and Methods: Candidate Kode Technology function‐spacer‐lipid (FSL) constructs were made for the Treponema pallidum lipoprotein (TmpA) of T. pallidum, using the peptide and FSL selection algorithms, and then used to make kodecytes. Developmental kodecytes were evaluated against a large range of syphilis antibody reactive and non‐reactive samples in column agglutination platforms and compared against established methodologies. Overall, 150 reactive and 2072 non‐reactive Syphicheck assay (a modified T. pallidum particle agglutination) blood donor samples were used to evaluate the agreement rate of the developed kodecyte assay. Results: From three FSL‐peptide candidate constructs, one was found to be the most suitable for diagnostics. Of 150 Syphicheck assay reactive samples, 146 were TmpA–kodecyte reactive (97.3% agreement), compared with 58.0% with the rapid plasmin reagin (RPR) assay for the same samples. Against the 2072 expected syphilis non‐reactive samples the agreement rate for TmpA–kodecytes was 98.8%. Conclusion: TmpA–kodecytes are viable for use as cost‐effective serologic reagent red cells for the detection of treponemal antibodies to diagnose syphilis with a high level of specificity in blood centres. This kodecyte methodology also potentially allows for introduction of the reverse‐algorithm testing into low‐volume laboratories, by utilizing existing transfusion laboratory infrastructure. [ABSTRACT FROM AUTHOR]

Published
2024
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19. Labeling of Polysaccharides with Biotin and Fluorescent Dyes

Author

Tuzikov, Alexander, primary, Shilova, Nadezhda, additional, Ovchinnikova, Tatiana, additional, Nokel, Alexey, additional, Patova, Olga, additional, Knirel, Yuriy, additional, Chernova, Tatiana, additional, Gorshkova, Tatiana, additional, and Bovin, Nicolai, additional

Published
2023
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21. Glycan-binding profile of DC-like cells

Author

Rapoport, Eugenia M., Moiseeva, Ekaterina V., Aronov, Dmitry A., Khaidukov, Sergey V., Pazynina, Galina V., Tsygankova, Svetlana V., Ryzhov, Ivan M., Belyanchikov, Ivan M., Tyrtysh, Tatiana V., McCullough, Kenneth C., and Bovin, Nicolai V.

Published
2020
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27. Labeling of Polysaccharides with Biotin and Fluorescent Dyes.

Author

Tuzikov, Alexander, Shilova, Nadezhda, Ovchinnikova, Tatiana, Nokel, Alexey, Patova, Olga, Knirel, Yuriy, Chernova, Tatiana, Gorshkova, Tatiana, and Bovin, Nicolai

Subjects
POLYSACCHARIDES, BIOTIN, FLUORESCEIN isothiocyanate, CARBOXYL group, HYALURONIC acid, GLYCOLIPIDS, FLUORESCENT dyes
Abstract

Examples of labeling polysaccharides at hydroxyl groups are described in this paper, which are especially in demand for molecules with a blocked reducing end. The protocols presented are suitable for the microscale synthesis of labeled polysaccharides that do not require a chromatography step for isolation. Examples of hydroxyl labeling include (1) direct modification with fluorescein isothiocyanate; (2) reaction with a fluorescein-dichlorotriazine derivative; (3) reaction with biotin-dichlorotriazine; (4) indirect two-step modification (given for glycosphingolipid) with glutaric anhydride followed by amidation with aminospacered BODIPY or SuCy5. The labeling of carboxyl groups of hyaluronic acid with BODIPY is also described. The staining of plant tissue sections with biotinylated polysaccharide versus being fluorescein labeled is compared. [ABSTRACT FROM AUTHOR]

Published
2024
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29. Printed Covalent Glycan Array for Ligand Profiling of Diverse Glycan Binding Proteins

Author

Blixt, Ola, Head, Steve, Mondala, Tony, Scanlan, Christopher, Huflejt, Margaret E., Alvarez, Richard, Bryan, Marian C., Fazio, Fabio, Calarese, Daniel, Stevens, James, Razi, Nahid, Stevens, David J., Skehel, John J., van Die, Irma, Burton, Dennis R., Wilson, Ian A., Cummings, Richard, Bovin, Nicolai, Wong, Chi-Huey, and Paulson, James C.

Published
2004

31. Removal of natural anti-αGal antibodies elicits protective immunity against Gram-negative bacterial infections

Author

Olivera-Ardid, Sara, primary, Bello-Gil, Daniel, additional, Perez-Cruz, Magdiel, additional, Costa, Cristina, additional, Camoez, Mariana, additional, Dominguez, M. Angeles, additional, Ferrero-Alves, Yara, additional, Vaquero, Jose Miguel, additional, Khasbiullina, Nailya, additional, Shilova, Nadezhda V., additional, Bovin, Nicolai V., additional, and Mañez, Rafael, additional

Published
2023
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32. Galectin-9 as a Potential Modulator of Lymphocyte Adhesion to Endothelium via Binding to Blood Group H Glycan

Author

Rapoport, Eugenia M., primary, Ryzhov, Ivan M., additional, Slivka, Ekaterina V., additional, Korchagina, Elena Yu., additional, Popova, Inna S., additional, Khaidukov, Sergey V., additional, André, Sabine, additional, Kaltner, Herbert, additional, Gabius, Hans-J., additional, Henry, Stephen, additional, and Bovin, Nicolai V., additional

Published
2023
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34. Protein Corona Attenuates the Targeting of Antitumor Sialyl Lewis X-Decorated Liposomes to Vascular Endothelial Cells under Flow Conditions

Author

Onishchenko, Natalia R., primary, Moskovtsev, Alexey A., additional, Kobanenko, Maria K., additional, Tretiakova, Daria S., additional, Alekseeva, Anna S., additional, Kolesov, Dmitry V., additional, Mikryukova, Anna A., additional, Boldyrev, Ivan A., additional, Kapkaeva, Marina R., additional, Shcheglovitova, Olga N., additional, Bovin, Nicolai V., additional, Kubatiev, Aslan A., additional, Tikhonova, Olga V., additional, and Vodovozova, Elena L., additional

Published
2023
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41. Natural Antibodies Against Sialoglycans

Author

Shilova, Nadezhda, Huflejt, Margaret E., Vuskovic, Marko, Obukhova, Polina, Navakouski, Maksim, Khasbiullina, Nailya, Pazynina, Galina, Galanina, Oxana, Bazhenov, Alexey, Bovin, Nicolai, Bayley, Hagan, Series editor, Houk, Kendall N., Series editor, Hughes, Greg, Series editor, Hunter, Christopher A., Series editor, Ishihara, Kazuaki, Series editor, Krische, Michael J, Series editor, Lehn, J.-M., Series editor, Luque, Rafael, Series editor, Olivucci, Massimo, Series editor, Siegel, Jay S., Series editor, Thiem, Joachim, Series editor, Venturi, Margherita, Series editor, Wong, Chi-Huey, Series editor, Wong, Henry N.C., Series editor, You, Shu-Li, Series editor, Wing-Wah Yam, Vivian, Series editor, Gerardy-Schahn, Rita, Delannoy, Philippe, and von Itzstein, Mark

Published
2015
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