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A Critical Site In The Core Of The Ccr5 Chemokine Receptor Required For Binding And Infectivity Of Human Immunodeficiency Virus Type 1, Salvatore J. Siciliano, Shawn E. Kuhmann, Youmin Weng, Navid Madani, Martin S. Springer, Janet E. Lineberger, Renee Danzeisen, Michael D. Miller, Michael Kavanaugh, Julie A. Demartino, David Kabat
A Critical Site In The Core Of The Ccr5 Chemokine Receptor Required For Binding And Infectivity Of Human Immunodeficiency Virus Type 1, Salvatore J. Siciliano, Shawn E. Kuhmann, Youmin Weng, Navid Madani, Martin S. Springer, Janet E. Lineberger, Renee Danzeisen, Michael D. Miller, Michael Kavanaugh, Julie A. Demartino, David Kabat
Biomedical and Pharmaceutical Sciences Faculty Publications
Like the CCR5 chemokine receptors of humans and rhesus macaques, the very homologous (∼98–99% identical) CCR5 of African green monkeys (AGMs) avidly binds β-chemokines and functions as a coreceptor for simian immunodeficiency viruses. However, AGM CCR5 is a weak coreceptor for tested macrophage-tropic (R5) isolates of human immunodeficiency virus type 1 (HIV-1). Correspondingly, gp120 envelope glycoproteins derived from R5 isolates of HIV-1 bind poorly to AGM CCR5. We focused on a unique extracellular amino acid substitution at the juncture of transmembrane helix 4 (TM4) and extracellular loop 2 (ECL2) (Arg for Gly at amino acid 163 (G163R)) as the likely …