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The N-Terminal V3 Loop Glycan Modulates the Interaction of Clade A and B Human Immunodeficiency Virus Type 1 Envelopes with CD4 and Chemokine Receptors

We investigated the underlying mechanism by which the highly conserved N-terminal V3 loop glycan of gp120 conferred resistance to neutralization of human immunodeficiency virus type 1 (HIV-1). We find that the presence or absence of this V3 glycan on clade A and B viruses accorded various degrees of...

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Библиографические подробности
Опубликовано в::J Virol
Главные авторы: Malenbaum, Susan E., Yang, David, Cavacini, Lisa, Posner, Marshall, Robinson, James, Cheng-Mayer, Cecilia
Формат: Artigo
Язык:Inglês
Опубликовано: American Society for Microbiology (ASM) 2000
Предметы:
Online-ссылка:https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC113181/
https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/11069996/
https://ncbi.nlm.nih.govhttps://doi.org/10.1128/jvi.74.23.11008-11016.2000
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