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• W1975223729 endingPage "8240" @default.
• W1975223729 startingPage "8227" @default.
• W1975223729 abstract "ABSTRACT Resistance to small-molecule CCR5 inhibitors arises when HIV-1 variants acquire the ability to use inhibitor-bound CCR5 while still recognizing free CCR5. Two isolates, CC101.19 and D1/85.16, became resistant via four substitutions in the gp120 V3 region and three in the gp41 fusion peptide (FP), respectively. The binding characteristics of a panel of monoclonal antibodies (MAbs) imply that several antigenic forms of CCR5 are expressed at different levels on the surfaces of U87-CD4-CCR5 cells and primary CD4 + T cells, in a cell-type-dependent manner. CCR5 binding and HIV-1 infection inhibition experiments suggest that the two CCR5 inhibitor-resistant viruses altered their interactions with CCR5 in different ways. As a result, both mutants became generally more sensitive to inhibition by CCR5 MAbs, and the FP mutant is specifically sensitive to a MAb that stains discrete cell surface clusters of CCR5 that may correspond to lipid rafts. We conclude that some MAbs detect different antigenic forms of CCR5 and that inhibitor-sensitive and -resistant viruses can use these CCR5 forms differently for entry in the presence or absence of CCR5 inhibitors." @default.
• W1975223729 created "2016-06-24" @default.
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• W1975223729 date "2011-08-15" @default.
• W1975223729 modified "2023-09-27" @default.
• W1975223729 title "Multiple CCR5 Conformations on the Cell Surface Are Used Differentially by Human Immunodeficiency Viruses Resistant or Sensitive to CCR5 Inhibitors" @default.
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• W1975223729 doi "https://doi.org/10.1128/jvi.00767-11" @default.
• W1975223729 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3147974" @default.
• W1975223729 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/21680525" @default.
• W1975223729 hasPublicationYear "2011" @default.
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