Abstract: Filling this cavity with a histidine or tryptophan residue in Env with a natural serine residue at this position (S375H/W) increased the susceptibility of HIV-1-infected cells to ADCC.
Abstract: In HIV-1, substitution of large residues such as histidine or tryptophan for serine 375 (S375H/W) in the gp120 Phe 43 cavity, where Phe 43 of CD4 contacts gp120, results in the spontaneous sampling of an Env conformation closer to the CD4-bound state.
Effects of the I559P gp41 change on the conformation and function of the human immunodeficiency virus (HIV-1) membrane envelope glycoprotein trimer.
Figure: In (C), recombinant HIV-1 bearing wt or S375W Envs
Figure: Normalized amounts of recombinant luciferase-expressing HIV-1 pseudotyped with the wt and S375W HIV-1BG505 Envs were incubated at 37 C with increasing concentrations (0-200 nM) of sCD4 (A) or VRC01 (B) for 1 hr prior to addition of Cf2Th-CD4/CCR5 cells.
Discussion: Compared with the wt HIV-1BG505 Env, the S375W mutant exhibited greater sensitivity to neutralization by sCD4, but not by the VRC01 CD4BS MAb.
Discussion: The S375W Env bound antibodies like 17b and A32, which prefer the CD4-bound conformation, more efficiently than the wt HIV-1BG505 Env, particularly in the presence of sCD4.
A model of peptide triazole entry inhibitor binding to HIV-1 gp120 and the mechanism of bridging sheet disruption.
Result: Previous work has shown that the parent peptide 12p1 does not inhibit binding of sCD4 to a mutant gp120 (S375W) that has a propensity to sample the activated/CD4-bound state , while it inhibits binding
Result: Previously, it was reported that a pocket-filling S375W mutation in gp120 completely abrogated binding of the parent 12p1 peptide .
Discussion: Interestingly, the S375W gp120 mutant was found to be resistant to the parent 12p1 peptide while we observed that S375A has reduced sensitivity to PTs (Figure 13).
Discussion: The significantly larger side chain of S375W would completely obstruct the critical peptide tryptophan from accessing contacts inside the F43 pocket.
MiniCD4 protein resistance mutations affect binding to the HIV-1 gp120 CD4 binding site and decrease entry efficiency.
Discussion: Furthermore, only the BaL viruses resistant towards M48U1 showed wild type levels of sensitivity towards sCD4, consistent with data published about the S375W mutation, while the other viruses showed some cross-resistance.
Characterization of human immunodeficiency virus type 1 monomeric and trimeric gp120 glycoproteins stabilized in the CD4-bound state: antigenicity, biophysics, and immunogenicity.
Abstract: Subsequently, we screened other mutations that, along with the S375W alteration, might further stabilize the CD4-bound state.
Abstract: The gp120 glycoproteins with the T257S-plus-S375W double mutation (T257S+S375W) have a superior antigenic profile compared to the originally identified single S375W replacement in terms of enhanced recognition by the broadly neutralizing CD4 binding-site antibody b12.
Abstract: The most conformationally constrained T257S+S375W trimeric gp120 proteins were selected for immunogenicity analysis in rabbits and displayed a trend of improvement relative to their wild-type counterparts in te
Characterization of the conformational state and flexibility of HIV-1 glycoprotein gp120 core domain.
PMID: 15131118
2004
The Journal of biological chemistry
Abstract: Toward this goal, we performed molecular dynamics simulations on the wild type gp120 core domain extracted from its ternary crystal structure and on a modeled mutant, S375W, that experimentally has a significantly different phenotype from the wild type.
HIV mutation literature information.
PMID: 
2017
Journal of virology
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