期刊
VIROLOGY
卷 401, 期 2, 页码 236-247出版社
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.virol.2010.02.019
关键词
HIV-1; Envelope glycoprotein; Glycosylation; DC-SIGN; Oligomannose; N-Acetylglucosaminyltransferase I
类别
资金
- AIDS fund (Amsterdam) [2005021, 2008013, 2009012]
- NIH [AI45463, AI36082, AI082362]
- International AIDS Vaccine Initiative
- Netherlands Organization for Scientific Research (NWO)
- American Foundation for AIDS Research (amfAR)
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.
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