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A Twin-cysteine Motif in the V2 Region of Gp120 is Associated with SIV Envelope Trimer Stabilization

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Journal PLoS One
Date 2013 Aug 13
PMID 23936006
Citations 14
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Abstract

The V1 and V2 variable regions of the primate immunodeficiency viruses contribute to the trimer association domain of the gp120 exterior envelope glycoprotein. A pair of V2 cysteine residues at 183 and 191 ("twin cysteines") is present in several simian immunodeficiency viruses, human immunodeficiency virus type 2 (HIV-2) and some SIV(cpz) lineages, but not in HIV-1. To examine the role of this potentially disulfide-bonded twin-cysteine motif, the cysteine residues in the SIVmac239 envelope glycoproteins were individually and pairwise substituted by alanine residues. All of the twin-cysteine mutants exhibited decreases in gp120 association with the Env trimer, membrane-fusing activity, and ability to support virus entry. Thus, the twin-cysteine motif plays a role in Env trimer stabilization in SIV and may do so in HIV-2 and some SIV(cpz) as well. This implies that HIV-1 lost the twin-cysteines, and may have relatively unstable Env trimers compared to SIV and HIV-2.

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References
1.
Barre-Sinoussi F, Chermann J, Rey F, Nugeyre M, Chamaret S, Gruest J . Isolation of a T-lymphotropic retrovirus from a patient at risk for acquired immune deficiency syndrome (AIDS). Science. 1983; 220(4599):868-71. DOI: 10.1126/science.6189183. View

2.
Julien J, Lee J, Cupo A, Murin C, Derking R, Hoffenberg S . Asymmetric recognition of the HIV-1 trimer by broadly neutralizing antibody PG9. Proc Natl Acad Sci U S A. 2013; 110(11):4351-6. PMC: 3600498. DOI: 10.1073/pnas.1217537110. View

3.
Moore P, Gray E, Sheward D, Madiga M, Ranchobe N, Lai Z . Potent and broad neutralization of HIV-1 subtype C by plasma antibodies targeting a quaternary epitope including residues in the V2 loop. J Virol. 2011; 85(7):3128-41. PMC: 3067856. DOI: 10.1128/JVI.02658-10. View

4.
Hu G, Liu J, Taylor K, Roux K . Structural comparison of HIV-1 envelope spikes with and without the V1/V2 loop. J Virol. 2010; 85(6):2741-50. PMC: 3067966. DOI: 10.1128/JVI.01612-10. View

5.
Pancera M, Majeed S, Ban Y, Chen L, Huang C, Kong L . Structure of HIV-1 gp120 with gp41-interactive region reveals layered envelope architecture and basis of conformational mobility. Proc Natl Acad Sci U S A. 2010; 107(3):1166-71. PMC: 2824281. DOI: 10.1073/pnas.0911004107. View