Lack of complex N-glycans on HIV-1 envelope glycoproteins preserves protein conformation and entry function
| العنوان: | Lack of complex N-glycans on HIV-1 envelope glycoproteins preserves protein conformation and entry function |
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| المؤلفون: | André M. Deelder, Ben Berkhout, William C. Olson, Mark Melchers, Valentin Le Douce, Dirk Eggink, Manfred Wuhrer, Cornelis H. Hokke, John P. Moore, Kathryn B. David, Antu K. Dey, Thijs van Montfort, Benno A. Naaijkens, Kenneth Kang, Rogier W. Sanders |
| المساهمون: | Medical Microbiology and Infection Prevention, AII - Amsterdam institute for Infection and Immunity |
| المصدر: | Virology, 401(2), 236-247 Virology, 401(2), 236-247. Academic Press Inc. |
| سنة النشر: | 2010 |
| مصطلحات موضوعية: | Models, Molecular, Antigenicity, Glycan, Glycosylation, Protein Conformation, viruses, Molecular Sequence Data, Mannose, Envelope glycoprotein, Biology, N-Acetylglucosaminyltransferases, Virus Replication, DC-SIGN, Article, Cell Line, chemistry.chemical_compound, Polysaccharides, Glycoprotein complex, Virology, N-Acetylglucosaminyltransferase I, Humans, chemistry.chemical_classification, Immunogenicity, env Gene Products, Human Immunodeficiency Virus, virus diseases, Virus Internalization, Recombinant Proteins, HIV-1 Envelope glycoprotein Glycosylation DC-SIGN Oligomannose N-Acetylglucosaminyltransferase I human-immunodeficiency-virus blue native electrophoresis cd4(+) t-lymphocytes hamster ovary cells dc-sign type-1 envelope antibody 2g12 neutralization epitope monoclonal-antibodies structural basis, Cell biology, carbohydrates (lipids), Carbohydrate Sequence, chemistry, HIV-1, biology.protein, Oligomannose, Glycoprotein |
| الوصف: | The HIV-1 envelope glycoprotein complex (Env) is the focus of vaccine development aimed at eliciting humoral immunity. Env's extensive and heterogeneous N-linked glycosylation affects folding, binding to lectin receptors, antigenicity and immunogenicity. We characterized recombinant Env proteins and virus particles produced in mammalian cells that lack N-acetylglucosaminyltransferase I (GnTI), an enzyme necessary for the conversion of oligomannose N-glycans to complex N-glycans. Carbohydrate analyses revealed that trimeric Env produced in GnTI(-/-) cells contained exclusively oligomannose N-glycans, with incompletely trimmed oligomannose glycans predominating. The folding and conformation of Env proteins was little affected by the manipulation of the glycosylation. Viruses produced in GnTI(-/-) cells were infectious, indicating that the conversion to complex glycans is not necessary for Env entry function, although virus binding to the C-type lectin DC-SIGN was enhanced. Manipulating Env's N-glycosylation may be useful for structural and functional studies and for vaccine design. (C) 2010 Elsevier Inc. All rights reserved. |
| اللغة: | English |
| تدمد: | 0042-6822 |
| URL الوصول: | https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e438911f4a21f9f8cf36ad3fca28baab http://hdl.handle.net/1887/109397 |
| Rights: | OPEN |
| رقم الانضمام: | edsair.doi.dedup.....e438911f4a21f9f8cf36ad3fca28baab |
| قاعدة البيانات: | OpenAIRE |
| تدمد: | 00426822 |
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