HIV-1 gp41 and TCRα Trans-Membrane Domains Share a Motif Exploited by the HIV Virus to Modulate T-Cell Proliferation

PLoS Pathogens

Niv Antonovsky¹  Tomer Cohen¹  Yechiel Shai¹  Irun R. Cohen²  Shmuel Jaffe Cohen² 

[1] Department of Biological Chemistry, the Weizmann Institute of Science, Rehovot, Israel;Department of Immunology, the Weizmann Institute of Science, Rehovot, Israel

关键词: T cells;    T cell receptors;    HIV-1;    Sequence alignment;    Antigen-presenting cells;    HIV;    Immunosuppressives;    Fluorescence resonance energy transfer;   

DOI  :  10.1371/journal.ppat.1001085

学科分类：生物科学（综合）

来源: Public Library of Science

【 摘 要 】

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 α-subunit of the T-cell receptor (TCRα). 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 TCRα and CD3 are localized to this nine amino acid motif within TCRα, and a peptide derived from it (TCRα 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 TCRα TMD and also from the other two known immunosuppressive regions within gp41.

【 授权许可】

CC BY