Cell surface ectodomain integrity of a subset of functional HIV-1 envelopes is dependent on a conserved hydrophilic domain containing region in their C-terminal tail. Retrovirology 2018;15(1):50 doi: 10.1186/s12977-018-0431-4
Scientific Publications
- PMID: 30029604
- Title: Cell surface ectodomain integrity of a subset of functional HIV 1 envelopes is dependent on a conserved hydrophilic domain containing region in their C terminal tail
- Abstract: HIV-1 Env gp160 is cleaved to form gp120 and gp41 and the functional HIV-1 Env is a trimer of non-covalently associated heterodimeric subunits, gp120 and gp41. The cleaved, native, trimeric form of Envs expose only broadly neutralizing antibody (bNAb) epitopes while occluding epitopes targeted by non-neutralizing antibodies (non-NAbs). We and others have previously observed that efficient cleavage of Envs into their constituent subunits co-relates with specific binding to bNAbs and poor binding to non-neutralizing antibodies (non-NAbs). Such Envs have been identified from clades A, B and C which make up a majority of globally circulating HIV-1 strains. Frequently, the C-terminal tail (CT) of Envs is deleted to enhance expression and stabilize soluble Env-based vaccine immunogens. Deletion of CT of efficiently cleaved Indian clade C Env 4-2.J41 results in recognition by both NAbs and non-NAbs. It is to be noted that uncleaved Envs bind to both NAbs and non-NAbs. So we investigated whether altered antigenicity upon CT deletion of efficiently cleaved Envs is due to inefficient cleavage or conformational change as the mechanism by which the CT regulates the ectodomain (ET) integrity is not well understood.
- Date: 1970-08-21
- Year: 2018
- Journal: Retrovirology
- PMID Author: Samal S, Das S, Boliar S, Qureshi H, Shrivastava T, Kumar N, Goswami S, Bansal M, Chakrabarti BK
- PMC Link #: PMC6053805
- IAVI Topics: HIV Immunogen Design
Cell surface ectodomain integrity of a subset of functional HIV 1 envelopes is dependent on a conserved hydrophilic domain containing region in their C terminal tail
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