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44
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of outstanding interest. A multi-cohort study that assessed the frequency of individuals homozygous and heterozygous for the Δ-32 CCR5 allele, in both HIV-1 infected and uninfected populations. The homozygous defect is present in about 1% of Caucasians, but is not found in other populations screened, and its presence is strongly associated with protection against HIV-1 infection. Heterozygozity for the Δ-32 CCR5 allele has only a modest protective effect against disease progression. See also [45].
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The role of a mutant CCR5 allele in HIV-1 transmission and disease progression
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of outstanding interest. A study conducted simultaneously with [44] that focuses on the Chicago component of the Multicenter AIDS Cohort Study group. This study draws similar conclusions to [44], notably that the homozygous Δ-32 CCR5 allele is strongly associated with protection against HIV-1 infection and that heterozygozity only moderately protects against disease progression.
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of special interest. A note that documents the existence of an HIV-1 infected Δ-32 CCR5 homozygote, while not providing details of the co-receptors used by the infecting HIV-1 strain, or its phenotype.
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CD4-induced interaction of primary HIV-1 gp120 glycoproteins with the chemokine receptor CCR-5
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of special interest. This study uses transfected, CCR5-expressing cells and an MIP-1β binding and competition assay to show that gp120 of M-tropic, but not T-tropic, HIV-1 isolates interacts with CCR5. The interaction is induced by soluble CD4, inhibited by anti-gp120 mAbs and is not dependent on sequences within the V1 or V2 loops of gp120. Direct binding of labelled gp120 to CCR5 is also demonstrated. See also [48].
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Wu L, Gerard NP, Wyatt R, Choe H, Parolin C, Ruffing N, Borsetti A, Cardoso AA, Desjardin E, Newman W, et al. CD4-induced interaction of primary HIV-1 gp120 glycoproteins with the chemokine receptor CCR-5. of special interest Nature. 384:1996;179-183 This study uses transfected, CCR5-expressing cells and an MIP-1β binding and competition assay to show that gp120 of M-tropic, but not T-tropic, HIV-1 isolates interacts with CCR5. The interaction is induced by soluble CD4, inhibited by anti-gp120 mAbs and is not dependent on sequences within the V1 or V2 loops of gp120. Direct binding of labelled gp120 to CCR5 is also demonstrated. See also [48].
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Wu, L.1
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CD4-dependent, antibody-sensitive interactions between HIV-1 and its co-receptor CCR5
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+ T cells to demonstrate that monomeric and oligomeric gp120 molecules from M-tropic, but not T-tropic, strains of HIV-1 genetic subtypes A, B and E interact with CCR5. CD4 binding is necessary for gp120 to bind to CCR5 with high affinity, and the interaction is inhibited by neutralizing, but not by non-neutralizing, anti-gp120 mAbs.
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+ T cells to demonstrate that monomeric and oligomeric gp120 molecules from M-tropic, but not T-tropic, strains of HIV-1 genetic subtypes A, B and E interact with CCR5. CD4 binding is necessary for gp120 to bind to CCR5 with high affinity, and the interaction is inhibited by neutralizing, but not by non-neutralizing, anti-gp120 mAbs.
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The lymphocyte chemoattractant SDF-1 is a ligand for LESTR/fusin and blocks HIV-1 entry
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The CXC chemokine SDF-1 is the ligand for LESTR/fusin and prevents infection by T-cell-line-adapted HIV-1
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