E-viri
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Herschhorn, Alon; Gu, Christopher; Moraca, Francesca; Ma, Xiaochu; Farrell, Mark; Smith, 3rd, Amos B; Pancera, Marie; Kwong, Peter D; Schön, Arne; Freire, Ernesto; Abrams, Cameron; Blanchard, Scott C; Mothes, Walther; Sodroski, Joseph G
Nature communications, 10/2017, Letnik: 8, Številka: 1Journal Article
The entry of HIV-1 into target cells is mediated by the viral envelope glycoproteins (Env). Binding to the CD4 receptor triggers a cascade of conformational changes in distant domains that move Env from a functionally "closed" State 1 to more "open" conformations, but the molecular mechanisms underlying allosteric regulation of these transitions are still elusive. Here, we develop chemical probes that block CD4-induced conformational changes in Env and use them to identify a potential control switch for Env structural rearrangements. We identify the gp120 β20-β21 element as a major regulator of Env transitions. Several amino acid changes in the β20-β21 base lead to open Env conformations, recapitulating the structural changes induced by CD4 binding. These HIV-1 mutants require less CD4 to infect cells and are relatively resistant to State 1-preferring broadly neutralizing antibodies. These data provide insights into the molecular mechanism and vulnerability of HIV-1 entry.
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JCR | SNIP | JCR | SNIP | JCR | SNIP | JCR | SNIP |
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in: SICRIS
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