ArticleFASEB journal : official publication of the Federation of American Societies for Experimental Biology2011
Viral envelope protein folding and membrane hemifusion are enhanced by the conserved loop region of HIV-1 gp41.
Article in FASEB journal : official publication of the Federation of American Societies for Experimental Biology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 18 citations in OpenAlex.
- An HIV-1 CRISPR-Cas9 membrane trafficking screen reveals a role for PICALM intersecting endolysosomes and immunity.iScience · 2024Article
- Role of Disulphide Bonds in Membrane Partitioning of a Viral Peptide.The Journal of membrane biology · 2022Review
- Molecular and Physicochemical Factors Governing Solubility of the HIV gp41 Ectodomain.Biophysical journal · 2016Article
- Disulfide Sensitivity in the Env Protein Underlies Lytic Inactivation of HIV-1 by Peptide Triazole Thiols.ACS chemical biology · 2015Article
- An immunomodulating motif of the HIV-1 fusion protein is chirality-independent: implications for its mode of action.The Journal of biological chemistry · 2013Article
- Structural and functional properties of the membranotropic HIV-1 glycoprotein gp41 loop region are modulated by its intrinsic hydrophobic core.The Journal of biological chemistry · 2013Article
- Immunoregulation through membrane proteins modified by reducing conditions induced by immune reactions.European journal of immunology · 2013Review
- HIV entry and envelope glycoprotein-mediated fusion.The Journal of biological chemistry · 2012Review
- HIV-1 induced bystander apoptosis.Viruses · 2012Review
- Exploiting topological constraints to reveal buried sequence motifs in the membrane-bound N-linked oligosaccharyl transferases.Biochemistry · 2011Article
Corrections and comments
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Authors and funding
5 authors at 3 institutions in 2 countries.
Funding
Abstract
Fusion of human immunodeficiency virus (HIV-1) with target cells is mediated by the gp41 transmembrane envelope protein. The loop region within gp41 contains 2 crucial cysteines that play an unknown role in HIV-cell fusion. On the basis of cell-cell fusion assay, using human T-cell lines [Jurkat E6-1 and Jurkat HXBc2(4)], and virus-cell fusion assay, using fully infectious HIV-1 HXBc2 virus and TZM-bl human cell line, we provide evidence that the oxidation state of the disulfide bond within a loop domain peptide determines its activity. The oxidized (closed) form inhibits fusion, while the reduced (opened) form enhances hemifusion. These opposite activities reach 60% difference in viral fusion. Both forms of the loop domain interact with gp41: the opened form enhances gp41 folding into a bundle, whereas the closed form inhibits this folding. Therefore, the transformation of the cysteines from a reduced to an oxidized state enables the loop to convert from opened to closed conformations, which assists gp41 to fold and induces hemifusion. The significant conservation of the loop region within many envelope proteins suggests a general mechanism, which is exploited by viruses to enhance entry into their host cells.
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