ArticlePLoS pathogens2010
HIV-1 gp41 and TCRalpha trans-membrane domains share a motif exploited by the HIV virus to modulate T-cell proliferation.
Article in PLoS pathogens, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 30 citations in OpenAlex.
- Mycoplasma genitalium Protein of Adhesion Suppresses T Cell Activation via CypA-CaN-NFAT Pathway.Microbiology spectrum · 2023Article
- The initial interplay between HIV and mucosal innate immunity.Frontiers in immunology · 2023Review
- Gp41 dynamically interacts with the TCR in the immune synapse and promotes early T cell activation.Scientific reports · 2018Article
- The HTLV-1 gp21 fusion peptide inhibits antigen specific T-cell activation in-vitro and in mice.PLoS pathogens · 2018Article
- Role of the HIV-1 envelope transmembrane domain in intracellular sorting.BMC cell biology · 2018Article
- Targeting Intramembrane Protein-Protein Interactions: Novel Therapeutic Strategy of Millions Years Old.Advances in protein chemistry and structural biology · 2018Review
- Effects of HIV-1 gp41-Derived Virucidal Peptides on Virus-like Lipid Membranes.Biophysical journal · 2017Article
- The Atomic Structure of the HIV-1 gp41 Transmembrane Domain and Its Connection to the Immunogenic Membrane-proximal External Region.The Journal of biological chemistry · 2015Article
- Conditional trimerization and lytic activity of HIV-1 gp41 variants containing the membrane-associated segments.Biochemistry · 2015Article
- Article
- Cholesterol-dependent membrane fusion induced by the gp41 membrane-proximal external region-transmembrane domain connection suggests a mechanism for broad HIV-1 neutralization.Journal of virology · 2014Article
- The HIV-1 envelope transmembrane domain binds TLR2 through a distinct dimerization motif and inhibits TLR2-mediated responses.PLoS pathogens · 2014Article
- An immunomodulating motif of the HIV-1 fusion protein is chirality-independent: implications for its mode of action.The Journal of biological chemistry · 2013Article
- The secret life of viral entry glycoproteins: moonlighting in immune evasion.PLoS pathogens · 2013Review
- A GxxxG-like motif within HIV-1 fusion peptide is critical to its immunosuppressant activity, structure, and interaction with the transmembrane domain of the T-cell receptor.The Journal of biological chemistry · 2012Article
- Drug efflux by a small multidrug resistance protein is inhibited by a transmembrane peptide.Antimicrobial agents and chemotherapy · 2012Article
- Rapid down-regulation of γc on T cells in early SIV infection correlates with impairment of T-cell function.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2012Article
- Evolution of immunity: no development without risk.Immunologic research · 2012Review
- HIV-1 gp41 transmembrane domain interacts with the fusion peptide: implication in lipid mixing and inhibition of virus-cell fusion.Biochemistry · 2012Article
- Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Viruses have evolved several strategies to modify cellular processes and evade the immune response in order to successfully infect, replicate, and persist in the host. By utilizing in-silico testing of a transmembrane sequence library derived from virus protein sequences, we have pin-pointed a nine amino-acid motif shared by a group of different viruses; this motif resembles the transmembrane domain of the alpha-subunit of the T-cell receptor (TCRalpha). The most striking similarity was found within the immunodeficiency virus (SIV and HIV) glycoprotein 41 TMD (gp41 TMD). Previous studies have shown that stable interactions between TCRalpha and CD3 are localized to this nine amino acid motif within TCRalpha, and a peptide derived from it (TCRalpha TMD, GLRILLLKV) interfered and intervened in the TCR function when added exogenously. We now report that the gp41 TMD peptide co-localizes with CD3 within the TCR complex and inhibits T cell proliferation in vitro. However, the inhibitory mechanism of gp41 TMD differs from that of the TCRalpha TMD and also from the other two known immunosuppressive regions within gp41.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.