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Article

HIV-1 clade C escapes broadly neutralizing autologous antibodies with N332 glycan specificity by distinct mechanisms.

Retrovirology - 30 Aug 2016

Deshpande Suprit, Patil Shilpa, Kumar Rajesh, Hermanus Tandile, Murugavel Kailapuri G, Srikrishnan Aylur K, Solomon Suniti, Morris Lynn, Bhattacharya Jayanta

Abstract excerpt

The glycan supersite centered on N332 in the V3 base of the HIV-1 envelope (Env) is a target for broadly neutralizing antibodies (bnAbs) such as PGT121 and PGT128. In this study, we examined the basis of resistance of HIV-1 clade C Envs obtained from broadly cross neutralizing (BCN) plasma of an Indian donor with N332 specificity. Pseudotyped viruses expressing autologous envs were found to be resistant to...

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Share to Antibodies, Neutralizing
Share to env Gene Products, Human Immunodeficiency Virus

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Share to HIV Envelope Protein gp120

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Source

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Identifiers

PMID: 27576440
DOI: 10.1186/s12977-016-0297-2
PMCID: PMC5006590

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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