Glycan microheterogeneity at the PGT135 antibody recognition site on HIV-1 gp120 reveals a molecular mechanism for neutralization resistance.

Journal article

Broadly neutralizing antibodies have been isolated that bind the glycan shield of the HIV-1 envelope spike. One such antibody, PGT135, contacts the intrinsic mannose patch of gp120 at the Asn332, Asn392, and Asn386 glycosylation sites. Here, site-specific glycosylation analysis of recombinant gp120 revealed glycan microheterogeneity sufficient to explain the existence of a minor population of virions resistant to PGT135 neutralization. Target microheterogeneity and antibody glycan specificity...

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Authors: Pritchard, L; Spencer, D; Royle, L; Vasiljevic, S; Krumm, S

• Publication status: Published
• Peer review status: Peer reviewed
• Publisher: American Society for Microbiology
• Journal: Journal of Virology
• Volume: 89
• Issue: 13
• Pages: 6952-6959
• Publication date: 2015-07-01
• Acceptance date: 2015-04-01
• DOI: 10.1128/jvi.00230-15
• EISSN: 1098-5514
• ISSN: 0022-538X
• Language: English
• Keywords: Antibodies, Neutralizing; HIV-1; HIV Antibodies; Polysaccharides; HIV Envelope Protein gp120; Immune Evasion