{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"volume":["111(19)"],"submitter":["Martinez-Munoz L"],"pubmed_abstract":["CCR5 and CXCR4, the respective cell surface coreceptors of R5 and X4 HIV-1 strains, both form heterodimers with CD4, the principal HIV-1 receptor. Using several resonance energy transfer techniques, we determined that CD4, CXCR4, and CCR5 formed heterotrimers, and that CCR5 coexpression altered the conformation of both CXCR4/CXCR4 homodimers and CD4/CXCR4 heterodimers. As a result, binding of the HIV-1 envelope protein gp120IIIB to the CD4/CXCR4/CCR5 heterooligomer was negligible, and the gp120-induced cytoskeletal rearrangements necessary for HIV-1 entry were prevented. CCR5 reduced HIV-1 envelope-induced CD4/CXCR4-mediated cell-cell fusion. In nucleofected Jurkat CD4 cells and primary human CD4(+) T cells, CCR5 expression led to a reduction in X4 HIV-1 infectivity. These findings can hel"],"journal":["Proceedings of the National Academy of Sciences of the United States of America"],"pagination":["E1960-9"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC4024905"],"repository":["biostudies-literature"],"pubmed_title":["CCR5/CD4/CXCR4 oligomerization prevents HIV-1 gp120IIIB binding to the cell surface."],"pmcid":["PMC4024905"],"pubmed_authors":["Rodriguez Frade JM","Barroso R","Vega B","Franco R","Dyrhaug SY","Santiago C","Costas C","Soriano SF","Navarro G","Martinez-Munoz L","Munoz-Fernandez MA","Lucas P","Mellado M"],"additional_accession":[]},"is_claimable":false,"name":"CCR5/CD4/CXCR4 oligomerization prevents HIV-1 gp120IIIB binding to the cell surface.","description":"CCR5 and CXCR4, the respective cell surface coreceptors of R5 and X4 HIV-1 strains, both form heterodimers with CD4, the principal HIV-1 receptor. Using several resonance energy transfer techniques, we determined that CD4, CXCR4, and CCR5 formed heterotrimers, and that CCR5 coexpression altered the conformation of both CXCR4/CXCR4 homodimers and CD4/CXCR4 heterodimers. As a result, binding of the HIV-1 envelope protein gp120IIIB to the CD4/CXCR4/CCR5 heterooligomer was negligible, and the gp120-induced cytoskeletal rearrangements necessary for HIV-1 entry were prevented. CCR5 reduced HIV-1 envelope-induced CD4/CXCR4-mediated cell-cell fusion. In nucleofected Jurkat CD4 cells and primary human CD4(+) T cells, CCR5 expression led to a reduction in X4 HIV-1 infectivity. These findings can hel","dates":{"release":"2014-01-01T00:00:00Z","publication":"2014 May","modification":"2025-04-05T13:37:09.638Z","creation":"2019-03-27T01:28:26Z"},"accession":"S-EPMC4024905","cross_references":{"pubmed":["24778234"],"doi":["10.1073/pnas.1322887111"]}}