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A conserved neutralizing epitope on gp41 of human immunodeficiency virus type 1
Since sequence variability of neutralizing epitopes is considered to be a major obstacle to HIV-1 vaccine development, the conserved B-cell epitope described here is a promising candidate for inclusion in a vaccine against AIDS.
CD4-dependent, antibody-sensitive interactions between HIV-1 and its co-receptor CCR-5
CD4 binding, although not absolutely necessary for the gp120–CCR-5 interaction, greatly increases its efficiency, and interference with HIV-1 binding to one or both of its receptors (CD4 and CCR-5) may be an important mechanism of virus neutralization.
Human monoclonal antibody 2G12 defines a distinctive neutralization epitope on the gp120 glycoprotein of human immunodeficiency virus type 1
Human monoclonal antibody 2G12 to the gp120 surface glycoprotein of human immunodeficiency virus type 1 (HIV-1) potently and broadly neutralizes primary and T-cell line-adapted clade B strains of HIV-1 and inhibits syncytium formation in the AA-2 cell line.
Generation of human monoclonal antibodies against HIV-1 proteins; electrofusion and Epstein-Barr virus transformation for peripheral blood lymphocyte immortalization.
Electrofusion turned out to be a more efficient immortalization method than EBV transformation, due to a high and constant immortalization rate, and the yield of stable specific hybridomas was increased twofold.
A binding pocket for a small molecule inhibitor of HIV-1 entry within the transmembrane helices of CCR5.
HIV-1 entry into CD4(+) cells requires the sequential interactions of the viral envelope glycoproteins with CD4 and a coreceptor such as the chemokine receptors CCR5 and CXCR4 to be blocked, and the TAK-779 molecule is explored.
Analysis of the Mechanism by Which the Small-Molecule CCR5 Antagonists SCH-351125 and SCH-350581 Inhibit Human Immunodeficiency Virus Type 1 Entry
The mechanism of action of two inhibitors of CCR5 function are identified, SCH-350581 (AD101) and SCH-351125 (SCH-C), which are more potent than SCH-C at inhibiting HIV-1 replication in primary lymphocytes, as well as viral entry and gp120 binding to cell lines.
HIV-1 escape from a small molecule, CCR5-specific entry inhibitor does not involve CXCR4 use
HIV-1 acquires the ability to use CCR5 despite the inhibitor, first by requiring lower levels of C CR5 for entry and then probably by using the drug-bound form of the receptor.
The BBXB Motif of RANTES Is the Principal Site for Heparin Binding and Controls Receptor Selectivity*
Mutation of the 44RKNR47 site reduced the selectivity of RANTES binding to different GAGs, and the triple 40s mutant was able to inhibit HIV-1 infectivity, but consistent with its abrogated GAG binding capacity, it no longer induced enhanced infectivity at high concentrations.
Co-receptors for HIV-1 entry.
A broadly neutralizing human monoclonal antibody against gp41 of human immunodeficiency virus type 1.
A hybridoma clone, designated 2F5, secreting a neutralizing human monoclonal antibody specific for gp41 of human immunodeficiency virus type 1 (HIV-1) showed broad-spectrum neutralizing capacity against HIV-1 laboratory isolates IIIB, MN, RF, and SF2.