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• W2043521256 abstract "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." @default.
• W2043521256 created "2016-06-24" @default.
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• W2043521256 date "2010-06-01" @default.
• W2043521256 modified "2023-09-23" @default.
• W2043521256 title "Lack of complex N-glycans on HIV-1 envelope glycoproteins preserves protein conformation and entry function" @default.
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• W2043521256 doi "https://doi.org/10.1016/j.virol.2010.02.019" @default.
• W2043521256 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3776475" @default.
• W2043521256 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/20304457" @default.
• W2043521256 hasPublicationYear "2010" @default.
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