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1. Absolute scattering length density profile of liposome bilayers obtained by SAXS combined with GIXOS: a tool to determine model biomembrane structure.

Author

Harvey, Richard D., Bello, Gianluca, Kikhney, Alexey G., Torres, Jaume, Surya, Wahyu, Wölk, Christian, and Shen, Chen

Subjects
SCATTERING (Physics), SMALL-angle X-ray scattering, LIPOSOMES, X-ray scattering, MEMBRANE lipids, BILAYER lipid membranes
Abstract

Lipid membranes play an essential role in biology, acting as host matrices for biomolecules like proteins and facilitating their functions. Their structures and structural responses to physiologically relevant interactions (i.e. with membrane proteins) provide key information for understanding biophysical mechanisms. Hence, there is a crucial need of methods to understand the effects of membrane host molecules on the lipid bilayer structure. Here, a purely experimental method is presented for obtaining the absolute scattering length density profile and the area per lipid of liposomal bilayers, by aiding the analysis of small‐angle X‐ray scattering (SAXS) data with the volume of bare headgroups obtained from grazing‐incidence X‐ray off‐specular scattering (GIXOS) data of monolayers of the same model membrane lipid composition. The GIXOS data experimentally demonstrate that the variation of the bare headgroup volume upon change in lipid packing density is small enough to allow its usage as a reference value without knowing the lipid packing stage in a bilayer. This approach also has the advantage that the reference volume is obtained in the same aqueous environment as used for the model membrane bilayers. The validity of this method is demonstrated using several typical membrane compositions, as well as one example of a phospholipid membrane with an incorporated transmembrane peptide. This methodology allows us to obtain absolute scale rather than relative scale values using solely X‐ray‐based instrumentation, retaining a similar resolution to SAXS experiments. The method presented has high potential for understanding the structural effects of membrane proteins on the biomembrane structure. [ABSTRACT FROM AUTHOR]

Published
2023
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4. Potent and selective bivalent inhibitors of BET bromodomains

Author

Waring, Michael J, Chen, Huawei, Rabow, Alfred A, Walker, Graeme, Bobby, Romel, Boiko, Scott, Bradbury, Rob H, Callis, Rowena, Clark, Edwin, Dale, Ian, Daniels, Danette L, Dulak, Austin, Flavell, Liz, Holdgate, Geoff, Jowitt, Thomas A, Kikhney, Alexey, McAlister, Mark, Méndez, Jacqui, Ogg, Derek, Patel, Joe, Petteruti, Philip, Robb, Graeme R, Robers, Matthew B, Saif, Sakina, Stratton, Natalie, Svergun, Dmitri I, Wang, Wenxian, Whittaker, David, Wilson, David M, and Yao, Yi

Published
2016
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9. WeNMR: Structural Biology on the Grid

Author

Wassenaar, Tsjerk A., van Dijk, Marc, Loureiro-Ferreira, Nuno, van der Schot, Gijs, de Vries, Sjoerd J., Schmitz, Christophe, van der Zwan, Johan, Boelens, Rolf, Giachetti, Andrea, Ferella, Lucio, Rosato, Antonio, Bertini, Ivano, Herrmann, Torsten, Jonker, Hendrik R. A., Bagaria, Anurag, Jaravine, Victor, Güntert, Peter, Schwalbe, Harald, Vranken, Wim F., Doreleijers, Jurgen F., Vriend, Gert, Vuister, Geerten W., Franke, Daniel, Kikhney, Alexey, Svergun, Dmitri I., Fogh, Rasmus H., Ionides, John, Laue, Ernest D., Spronk, Chris, Jurkša, Simonas, Verlato, Marco, Badoer, Simone, Dal Pra, Stefano, Mazzucato, Mirco, Frizziero, Eric, and Bonvin, Alexandre M. J. J.

Published
2012
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11. ATSAS 3.0: expanded functionality and new tools for small-angle scattering data analysis

Author

Manalastas-Cantos, Karen, Konarev, Petr V., Hajizadeh, Nelly R., Kikhney, Alexey G., Molodenskiy, Dmitry S., Panjkovich, Alejandro, Mertens, Haydyn D. T., Gruzinov, Andrey, and Borges, Clemente

Subjects
small-angle scattering, ATSAS, data analysis, structural modelling, biological macromolecules
Abstract

The ATSAS software suite encompasses a number of programs for the processing, visualization, analysis and modelling of small-angle scattering data, with a focus on the data measured from biological macromolecules. Here, new developments in the ATSAS 3.0 package are described. They include IMSIM, for simulating isotropic 2D scattering patterns; IMOP, to perform operations on 2D images and masks; DATRESAMPLE, a method for variance estimation of structural invariants through parametric resampling; DATFT, which computes the pair distance distribution function by a direct Fourier transform of the scattering data; PDDFFIT, to compute the scattering data from a pair distance distribution function, allowing comparison with the experimental data; a new module in DATMW for Bayesian consensus-based concentration-independent molecular weight estimation; DATMIF, an ab initio shape analysis method that optimizes the search model directly against the scattering data; DAMEMB, an application to set up the initial search volume for multiphase modelling of membrane proteins; ELLLIP, to perform quasi-atomistic modelling of liposomes with elliptical shapes; NMATOR, which models conformational changes in nucleic acid structures through normal mode analysis in torsion angle space; DAMMIX, which reconstructs the shape of an unknown intermediate in an evolving system; and LIPMIX and BILMIX, for modelling multilamellar and asymmetric lipid vesicles, respectively. In addition, technical updates were deployed to facilitate maintainability of the package, which include porting the PRIMUS graphical interface to Qt5, updating SASpy – a PyMOL plugin to run a subset of ATSAS tools – to be both Python 2 and 3 compatible, and adding utilities to facilitate mmCIF compatibility in future ATSAS releases. All these features are implemented in ATSAS 3.0, freely available for academic users at https://www.embl-hamburg.de/biosaxs/software.html., Journal of Applied Crystallography, 54, ISSN:0021-8898, ISSN:1600-5767

Published
2021

12. Anomalous small-angle X-ray scattering on biological macromolecules at the P12 beamline of EMBL-Hamburg

Author

Gruzinov, Andrey, Schroer, Martin, Blanchet, Clement, Manalastas-Cantos, Karen, Kikhney, Alexey, Hajizadeh, Nelly, Wieland, Florian, Schulz, Florian, Franke, Daniel, Jeffries, Cy, and Svergun, Dmitri

Subjects
Inorganic Chemistry, Structural Biology, General Materials Science, ddc:530, Physical and Theoretical Chemistry, Condensed Matter Physics, Biochemistry
Abstract

Acta crystallographica / A 77(a2), C290 - C290 (2021). doi:10.1107/S0108767321093922, Published by Blackwell, Oxford [u.a.]

Published
2021
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15. A Giant Extracellular Matrix Binding Protein of Staphylococcus epidermidis Binds Surface-Immobilized Fibronectin via a Novel Mechanism

Author

Büttner, Henning, primary, Perbandt, Markus, additional, Kohler, Thomas, additional, Kikhney, Alexey, additional, Wolters, Manuel, additional, Christner, Martin, additional, Heise, Marisol, additional, Wilde, Jérôme, additional, Weißelberg, Samira, additional, Both, Anna, additional, Betzel, Christian, additional, Hammerschmidt, Sven, additional, Svergun, Dmitri, additional, Aepfelbacher, Martin, additional, and Rohde, Holger, additional

Published
2020
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18. SASBDB: Towards an automatically curated and validated repository for biological scattering data.

Author

Kikhney, Alexey G., Borges, Clemente R., Molodenskiy, Dmitry S., Jeffries, Cy M., and Svergun, Dmitri I.

Abstract

Small‐angle scattering (SAS) of X‐rays and neutrons is a fundamental tool to study the nanostructural properties, and in particular, biological macromolecules in solution. In structural biology, SAS recently transformed from a specialization into a general technique leading to a dramatic increase in the number of publications reporting structural models. The growing amount of data recorded and published has led to an urgent need for a global SAS repository that includes both primary data and models. In response to this, a small‐angle scattering biological data bank (SASBDB) was designed in 2014 and is available for public access at www.sasbdb.org. SASBDB is a comprehensive, free and searchable repository of SAS experimental data and models deposited together with the relevant experimental conditions, sample details and instrument characteristics. SASBDB is rapidly growing, and presently has over 1,000 entries containing more than 1,600 models. We describe here the overall organization and procedures of SASBDB paying most attention to user‐relevant information during submission. Perspectives of further developments, in particular, with OneDep system of the Protein Data Bank, and also widening of SASBDB including new types of data/models are discussed. [ABSTRACT FROM AUTHOR]

Published
2020
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23. Macromolecular pHPMA-Based Nanoparticles with Cholesterol for Solid Tumor Targeting: Behavior in HSA Protein Environment

Author

Zhang, Xiaohan, Niebuur, Bart-Jan, Chytil, Petr, Etrych, Tomas, Filippov, Sergey K., Kikhney, Alexey, Wieland, D. C. Florian, Svergun, Dmitri I., and Papadakis, Christine M.

Abstract

Nanoparticles (NPs) that form by self-assembly of amphiphilic poly(N-(2-hydroxypropyl)-methacrylamide) (pHPMA) copolymers bearing cholesterol side groups are potential drug carriers for solid tumor treatment. Here, we investigate their behavior in solutions of human serum albumin (HSA) in phosphate buffered saline. Mixed solutions of NPs, from polymer conjugates with or without the anticancer drug doxorubicin (Dox) bound to them, and HSA at concentrations up to the physiological value are characterized by synchrotron small-angle X-ray scattering and isothermal titration calorimetry. When Dox is absent, a small amount of HSA molecules bind to the cholesterol groups that form the core of the NPs by diffusing through the loose pHPMA shell or get caught in meshes formed by the pHPMA chains. These interactions are strongly hindered by the presence of Dox, which is distributed in the pHPMA shell, meaning that the delivery of Dox by the NPs in the human body is not affected by the presence of HSA.

Published
2024
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24. The BR domain of PsrP interacts with extracellular DNA to promote bacterial aggregation; structural insights into pneumococcal biofilm formation

Author

Schulte, Tim, Mikaelsson, Cecilia, Beaussart, Audrey, Kikhney, Alexey, Deshmukh, Maya, Wolniak, Sebastian, Pathak, Anuj, Ebel, Christine, Lofling, Jonas, Fogolari, Federico, Henriques-Normark, Birgitta, Dufrene, Yves F., Svergun, Dmitri, Nygren, Per-Ake, Achour, Adnane, Schulte, Tim, Mikaelsson, Cecilia, Beaussart, Audrey, Kikhney, Alexey, Deshmukh, Maya, Wolniak, Sebastian, Pathak, Anuj, Ebel, Christine, Lofling, Jonas, Fogolari, Federico, Henriques-Normark, Birgitta, Dufrene, Yves F., Svergun, Dmitri, Nygren, Per-Ake, and Achour, Adnane

Abstract

The major human pathogen Streptococcus pneumoniae is a leading cause of disease and death worldwide. Pneumococcal biofilm formation within the nasopharynx leads to long-term colonization and persistence within the host. We have previously demonstrated that the capsular surface-associated pneumococcal serine rich repeat protein (PsrP), key factor for biofilm formation, binds to keratin-10 (KRT10) through its microbial surface component recognizing adhesive matrix molecule (MSCRAMM)-related globular binding region domain (BR187-385). Here, we show that BR187-385 also binds to DNA, as demonstrated by electrophoretic mobility shift assays and size exclusion chromatography. Further, heterologous expression of BR187-378 or the longer BR120-378 construct on the surface of a Gram-positive model host bacterium resulted in the formation of cellular aggregates that was significantly enhanced in the presence of DNA. Crystal structure analyses revealed the formation of BR187-385 homo-dimers via an intermolecular beta-sheet, resulting in a positively charged concave surface, shaped to accommodate the acidic helical DNA structure. Furthermore, small angle X-ray scattering and circular dichroism studies indicate that the aggregate-enhancing N-terminal region of BR120-166 adopts an extended, non-globular structure. Altogether, our results suggest that PsrP adheres to extracellular DNA in the biofilm matrix and thus promotes pneumococcal biofilm formation., QC 20161012

Published
2016
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25. The BR domain of PsrP interacts with extracellular DNA to promote bacterial aggregation; structural insights into pneumococcal biofilm formation

Author

Schulte, Tim, primary, Mikaelsson, Cecilia, additional, Beaussart, Audrey, additional, Kikhney, Alexey, additional, Deshmukh, Maya, additional, Wolniak, Sebastian, additional, Pathak, Anuj, additional, Ebel, Christine, additional, Löfling, Jonas, additional, Fogolari, Federico, additional, Henriques-Normark, Birgitta, additional, Dufrêne, Yves F., additional, Svergun, Dmitri, additional, Nygren, Per-Åke, additional, and Achour, Adnane, additional

Published
2016
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26. Immunosuppressive Yersinia Effector YopM Binds DEAD Box Helicase DDX3 to Control Ribosomal S6 Kinase in the Nucleus of Host Cells

Author

Berneking, Laura, primary, Schnapp, Marie, additional, Rumm, Andreas, additional, Trasak, Claudia, additional, Ruckdeschel, Klaus, additional, Alawi, Malik, additional, Grundhoff, Adam, additional, Kikhney, Alexey G., additional, Koch-Nolte, Friedrich, additional, Buck, Friedrich, additional, Perbandt, Markus, additional, Betzel, Christian, additional, Svergun, Dmitri I., additional, Hentschke, Moritz, additional, and Aepfelbacher, Martin, additional

Published
2016
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28. Structure of ThiM from Vitamin B1 biosynthetic pathway of Staphylococcus aureus – Insights into a novel pro-drug approach addressing MRSA infections

Author

Drebes, Julia, primary, Künz, Madeleine, additional, Windshügel, Björn, additional, Kikhney, Alexey G., additional, Müller, Ingrid B., additional, Eberle, Raphael J., additional, Oberthür, Dominik, additional, Cang, Huaixing, additional, Svergun, Dmitri I., additional, Perbandt, Markus, additional, Betzel, Christian, additional, and Wrenger, Carsten, additional

Published
2016
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33. The keratin-10 binding region of the pneumococcal serine rich repeat protein (PsrP) forms a domain-swapped dimer and intermolecular β-sheets – implications for biofilm formation ofStreptococcus pneumoniae

Author

Schulte, Tim, primary, Löfling, Jonas, additional, Mikaelsson, Cecilia, additional, Kikhney, Alexey, additional, Hentrich, Karina, additional, Diamante, Aurora, additional, Ebel, Christine, additional, Normark, Staffan, additional, Svergun, Dmitri, additional, Henriques-Normark, Birgitta, additional, and Achour, Adnane, additional

Published
2015
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35. Versatile sample environments and automation for biological solution X-ray scattering experiments at the P12 beamline (PETRA III, DESY)

Author

Blanchet, Clement E., primary, Spilotros, Alessandro, additional, Schwemmer, Frank, additional, Graewert, Melissa A., additional, Kikhney, Alexey, additional, Jeffries, Cy M., additional, Franke, Daniel, additional, Mark, Daniel, additional, Zengerle, Roland, additional, Cipriani, Florent, additional, Fiedler, Stefan, additional, Roessle, Manfred, additional, and Svergun, Dmitri I., additional

Published
2015
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36. Structural and Functional Insights into Peptidoglycan Access for the Lytic Amidase LytA of Streptococcus pneumoniae

Author

Mellroth, Peter, Sandalova, Tatyana, Kikhney, Alexey, Vilaplana, Francisco, Hesek, Dusan, Lee, Mijoon, Mobashery, Shahriar, Normark, Staffan, Svergun, Dmitri, Henriques-Normark, Birgitta, Achour, Adnane, Mellroth, Peter, Sandalova, Tatyana, Kikhney, Alexey, Vilaplana, Francisco, Hesek, Dusan, Lee, Mijoon, Mobashery, Shahriar, Normark, Staffan, Svergun, Dmitri, Henriques-Normark, Birgitta, and Achour, Adnane

Abstract

The cytosolic N-acetylmuramoyl-L-alanine amidase LytA protein of Streptococcus pneumoniae, which is released by bacterial lysis, associates with the cell wall via its choline-binding motif. During exponential growth, LytA accesses its peptidoglycan substrate to cause lysis only when nascent peptidoglycan synthesis is stalled by nutrient starvation or beta-lactam antibiotics. Here we present three-dimensional structures of LytA and establish the requirements for substrate binding and catalytic activity. The solution structure of the full-length LytA dimer reveals a peculiar fold, with the choline-binding domains forming a rigid V-shaped scaffold and the relatively more flexible amidase domains attached in a trans position. The 1.05-angstrom crystal structure of the amidase domain reveals a prominent Y-shaped binding crevice composed of three contiguous subregions, with a zinc-containing active site localized at the bottom of the branch point. Site-directed mutagenesis was employed to identify catalytic residues and to investigate the relative impact of potential substrate-interacting residues lining the binding crevice for the lytic activity of LytA. In vitro activity assays using defined muropeptide substrates reveal that LytA utilizes a large substrate recognition interface and requires large muropeptide substrates with several connected saccharides that interact with all subregions of the binding crevice for catalysis. We hypothesize that the substrate requirements restrict LytA to the sites on the cell wall where nascent peptidoglycan synthesis occurs. IMPORTANCE Streptococcus pneumoniae is a human respiratory tract pathogen responsible for millions of deaths annually. Its major pneumococcal autolysin, LytA, is required for autolysis and fratricidal lysis and functions as a virulence factor that facilitates the spread of toxins and factors involved in immune evasion. LytA is also activated by penicillin and vancomycin and is responsible for the lysis induced by t, QC 20140424

Published
2014
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37. Designing a Multimer Allergen for Diagnosis and Immunotherapy of Dog Allergic Patients

Author

Nilsson, Ola B., Neimert-Andersson, Theresa, Bronge, Mattias, Grundström, Jeanette, Sarma, Ranjana, Uchtenhagen, Hannes, Kikhney, Alexey, Sandalova, Tatyana, Holmgren, Erik, Svergun, Dmitri, Achour, Adnane, van Hage, Marianne, Grönlund, Hans, Nilsson, Ola B., Neimert-Andersson, Theresa, Bronge, Mattias, Grundström, Jeanette, Sarma, Ranjana, Uchtenhagen, Hannes, Kikhney, Alexey, Sandalova, Tatyana, Holmgren, Erik, Svergun, Dmitri, Achour, Adnane, van Hage, Marianne, and Grönlund, Hans

Abstract

Background: Dog dander extract used for diagnosis and allergen-specific immunotherapy is often of variable and of poor quality. Objective: To assemble four well-established dog allergen components into one recombinant folded protein for improved diagnosis and vaccination of allergy to dog. Methods: A linked molecule, comprising the four dog lipocalin allergens Can f 1, Can f 2, Can f 4 and Can f 6 was constructed. The tetrameric protein was structurally characterized by small angle X-ray scattering, and compared with each single recombinant lipocalin allergen or an equimolar mix of the four allergens by analytical size exclusion chromatography, circular dichroism, allergen-specific IgE in serum by ELISA and allergen-dependent capacity to activate basophils. The immunogenicity of the fusion protein was evaluated in immunized mice by assessing splenocyte proliferation and antibody production. Results: The linked tetrameric construct was produced as a soluble fusion protein, with the specific folds of the four individual allergens conserved. This multi-allergen molecule was significantly more efficient (p < 0.001) than each single recombinant allergen in binding to dog-specific IgE, and the epitope spectrum was unaffected compared to an equimolar mix of the four allergens. Basophil degranulation revealed that the biologic activity of the linked molecule was retained. Immunization of mice with the linked construct induced comparable allergen-specific IgG responses with blocking capacity towards all included allergens and generated comparably low T-cell responses. Conclusion: We provide the first evidence for a linked recombinant molecule covering the major dog allergens for potential use in diagnostics and allergy vaccination of dog allergic patients.

Published
2014
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38. Designing a Multimer Allergen for Diagnosis and Immunotherapy of Dog Allergic Patients

Author

Nilsson, Ola B., primary, Neimert-Andersson, Theresa, additional, Bronge, Mattias, additional, Grundström, Jeanette, additional, Sarma, Ranjana, additional, Uchtenhagen, Hannes, additional, Kikhney, Alexey, additional, Sandalova, Tatyana, additional, Holmgren, Erik, additional, Svergun, Dmitri, additional, Achour, Adnane, additional, van Hage, Marianne, additional, and Grönlund, Hans, additional

Published
2014
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40. Correction to ‘The basic keratin 10-binding domain of the virulence-associated pneumococcal serine-rich protein PsrP adopts a novel MSCRAMM fold’

Author

Schulte, Tim, primary, Löfling, Jonas, additional, Mikaelsson, Cecilia, additional, Kikhney, Alexey, additional, Hentrich, Karina, additional, Diamante, Aurora, additional, Ebel, Christine, additional, Normark, Staffan, additional, Svergun, Dmitri, additional, Henriques-Normark, Birgitta, additional, and Achour, Adnane, additional

Published
2014
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41. Structural and Functional Insights into Peptidoglycan Access for the Lytic Amidase LytA of Streptococcus pneumoniae

Author

Mellroth, Peter, primary, Sandalova, Tatyana, additional, Kikhney, Alexey, additional, Vilaplana, Francisco, additional, Hesek, Dusan, additional, Lee, Mijoon, additional, Mobashery, Shahriar, additional, Normark, Staffan, additional, Svergun, Dmitri, additional, Henriques-Normark, Birgitta, additional, and Achour, Adnane, additional

Published
2014
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42. The basic keratin 10-binding domain of the virulence-associated pneumococcal serine-rich protein PsrP adopts a novel MSCRAMM fold

Author

Schulte, Tim, primary, Löfling, Jonas, additional, Mikaelsson, Cecilia, additional, Kikhney, Alexey, additional, Hentrich, Karina, additional, Diamante, Aurora, additional, Ebel, Christine, additional, Normark, Staffan, additional, Svergun, Dmitri, additional, Henriques-Normark, Birgitta, additional, and Achour, Adnane, additional

Published
2014
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43. Designing a Multimer Allergen for Diagnosis and Immunotherapy of Dog Allergic Patients

Author

Lai, Hsin-Chih, Neimert-Andersson, Theresa, Achour, Adnane, van Hage, Marianne, Grönlund, Hans, Bronge, Mattias, Grundström, Jeanette, Sarma, Ranjana, Uchtenhagen, Hannes, Kikhney, Alexey, Sandalova, Tatyana, Holmgren, Erik, and Svergun, Dmitri

Subjects
Allergy, Immunoglobulin E, medicine.disease_cause, Biochemistry, Epitope, Mice, Allergen, immune system diseases, Allergies, Medicine and Health Sciences, Mice, Inbred BALB C, Dander, Multidisciplinary, biology, Chemistry, Immunogenicity, respiratory system, Lipocalins, Recombinant Proteins, 3. Good health, Medicine, Female, ddc:500, Immunotherapy, Antibody, Research Article, Protein Structure, Science, Immunology, Basophil degranulation, Antibodies, Diagnostic Medicine, Hypersensitivity, otorhinolaryngologic diseases, medicine, Animals, Humans, Biology and Life Sciences, Proteins, Allergens, medicine.disease, Fusion protein, respiratory tract diseases, Allergy Immunotherapy, biology.protein, Clinical Immunology, Protein Multimerization, Clinical Medicine
Abstract

BackgroundDog dander extract used for diagnosis and allergen-specific immunotherapy is often of variable and of poor quality.ObjectiveTo assemble four well-established dog allergen components into one recombinant folded protein for improved diagnosis and vaccination of allergy to dog.MethodsA linked molecule, comprising the four dog lipocalin allergens Can f 1, Can f 2, Can f 4 and Can f 6 was constructed. The tetrameric protein was structurally characterized by small angle X-ray scattering, and compared with each single recombinant lipocalin allergen or an equimolar mix of the four allergens by analytical size exclusion chromatography, circular dichroism, allergen-specific IgE in serum by ELISA and allergen-dependent capacity to activate basophils. The immunogenicity of the fusion protein was evaluated in immunized mice by assessing splenocyte proliferation and antibody production.ResultsThe linked tetrameric construct was produced as a soluble fusion protein, with the specific folds of the four individual allergens conserved. This multi-allergen molecule was significantly more efficient (pConclusionWe provide the first evidence for a linked recombinant molecule covering the major dog allergens for potential use in diagnostics and allergy vaccination of dog allergic patients.

Published
2014

44. Peroxisomal Proteostasis Involves a Lon Family Protein That Functions as Protease and Chaperone

Author

Bartoszewska, Magdalena, Williams, Chris, Kikhney, Alexey, Opalinski, Lukasz, van Roermund, Carlo W. T., de Boer, Rinse, Veenhuis, Marten, van der Klei, Ida J., Bartoszewska, Magdalena, Williams, Chris, Kikhney, Alexey, Opalinski, Lukasz, van Roermund, Carlo W. T., de Boer, Rinse, Veenhuis, Marten, and van der Klei, Ida J.

Abstract

Proteins are subject to continuous quality control for optimal proteostasis. The knowledge of peroxisome quality control systems is still in its infancy. Here we show that peroxisomes contain a member of the Lon family of proteases (Pln). We show that Pln is a heptameric protein and acts as an ATP-fueled protease and chaperone. Hence, Pln is the first chaperone identified in fungal peroxisomes. In cells of a PLN deletion strain peroxisomes contain protein aggregates, a major component of which is catalase-peroxidase. We show that this enzyme is sensitive to oxidative damage. The oxidatively damaged, but not the native protein, is a substrate of the Pln protease. Cells of the pln strain contain enhanced levels of catalase-peroxidase protein but reduced catalase-peroxidase enzyme activities. Together with the observation that Pln has chaperone activity in vitro, our data suggest that catalase-peroxidase aggregates accumulate in peroxisomes of pln cells due to the combined absence of Pln protease and chaperone activities.

Published
2012

49. Instrumental setup for high-throughput small- and wide-angle solution scattering at the X33 beamline of EMBL Hamburg

Author

Blanchet, Clement E., primary, Zozulya, Alexey V., additional, Kikhney, Alexey G., additional, Franke, Daniel, additional, Konarev, Peter V., additional, Shang, Weifeng, additional, Klaering, Robbert, additional, Robrahn, Bernd, additional, Hermes, Christoph, additional, Cipriani, Florent, additional, Svergun, Dmitri I., additional, and Roessle, Manfred, additional

Published
2012
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