Enhanced exposure of human immunodeficiency virus type 1 primary isolate neutralization epitopes through binding of CD4 mimetic compounds.

N-(4-Chlorophenyl)-N'-(2,2,6,6-tetramethyl-piperidin-4-yl)-oxalamide (NBD-556) is a low-molecular-weight compound that reportedly blocks the interaction between human immunodeficiency virus type 1 (HIV-1) gp120 and its receptor CD4. We investigated whether the enhancement of binding of anti-gp120 monoclonal antibodies (MAbs) toward envelope (Env) protein with NBD-556 are similar to those of soluble CD4 (sCD4) by comparing the binding profiles of the individual MAbs to Env-expressing cell surfaces. In flow cytometric analyses, the binding profiles of anti-CD4-induced epitope (CD4i) MAbs toward NBD-556-pretreated Env-expressing cell surfaces were similar to the binding profiles toward sCD4-pretreated cell surfaces.

Human immunodeficiency virus type 1 evasion of a neutralizing anti-V3 antibody involves acquisition of a potential glycosylation site in V2.

It has been reported that the addition of a potential N-linked glycosylation site (PNGS) to the gp120 human immunodeficiency virus type 1 (HIV-1) envelope glycoprotein provides protection against neutralizing antibodies (NAbs) by acting as a 'glycan shield'. In this study, we induced insertion of a PNGS into the V2 region of HIV-1(BaL) with the KD-247 anti-V3 neutralizing monoclonal antibody. In the presence of KD-247 (200 microg ml(-1)) at passage five, viruses with 3 aa mutations in the C2 (T240S and I283T) and V3 (T319A) regions expanded from pre-existing variants.