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Envelope surface glycoprotein gp120
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env
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HIV-1 gp120 and gp41-mediated virus-cell fusion is more dependent on viral core maturation for viruses bearing CXCR4-tropic gp120 than for those bearing CCR5-tropic gp120 |
PubMed
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env
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The coreceptor-binding site in HIV-1 gp120 is centered around an anti-parallel beta-sheet structure "bridging sheet domain"; mutations in and adjacent to this domain have greater impact on CXCR4-mediated fusion than on CCR5-mediated fusion |
PubMed
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env
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The V3 domain of HIV-1 gp120 induces associations between CD4 and CCR5 receptors in cholesterol-rich microenvironments |
PubMed
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env
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HIV-1 gp120 induced cell death is inhibited by a CCR5-mediated neuroprotective pathway that involves protein kinase Akt/PKB as an essential component and can be triggered by the CCR5 agonists MIP-1beta and RANTES |
PubMed
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env
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HIV-1 gp120-induced neuronal cell death involves p38 mitogen-activated protein kinase; both HIV-1 coreceptors, CCR5 and CXCR4, can mediate HIV-1 gp120-induced neurotoxicity |
PubMed
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env
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Stimulation of human monocyte-derived macrophages with HIV-1 gp120 results in the CCR5-mediated activation of Lyn and the concomitant Lyn-dependent activation of the mitogen-activated protein (MAP) kinase ERK-1/2, which leads to production of TNF-alpha |
PubMed
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env
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HIV-1 gp120-induced Ca(2+) fluxing is CD4 dependent and coreceptor specific, and is mediated by the CCR5 and CXCR4 coreceptors |
PubMed
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env
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HIV-1 gp120 from a T-cell-tropic virus causes CD4-dependent antagonism of CXCR4 response to SDF-1alpha, whereas gp120 from macrophage-tropic viruses causes CD4-dependent antagonism of CCR5 response to MIP-1alpha |
PubMed
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env
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In addition to the V3 loop of HIV-1 gp120, some conserved amino acid residues (117-123, 207, 419-422, and 438-441) are also involved in CCR5 chemokine receptor binding |
PubMed
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env
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The amino-terminal residues (amino acids 1-25) and three extracellular loops (amino acids 88-102, 168-194, 261-277) of the CCR5 coreceptor are highly involved in its binding to gp120 from macrophage-tropic HIV-1 strains and in CCR5-mediated HIV-1 entry |
PubMed
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env
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A peptide fragment corresponding to the loop between the fifth and sixth transmembrane regions of the CCR5 receptor (amino acids 222-240) can inhibit HIV-1 infection of MT-4 cells, suggesting this region of CCR5 is involved with HIV-1 gp120 binding |
PubMed
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env
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A synthetic peptide corresponding to amino acid residues 414-434 of HIV-1 gp120 downregulates the expression and function of chemokine receptors CCR5 and CXCR4 in monocytes by activating the 7-transmembrane G-protein-coupled receptor FPRL1/LXA4R |
PubMed
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env
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Chemokines such as MCP-3 and MCP-2 that can compete with high affinity for MIP-1beta binding to CCR5 can also compete for monomeric HIV-1 gp120 binding to CCR5, although with variable potencies |
PubMed
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env
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An adapted primary HIV-1 isolate, ADA, is able to replicate in CD4-negative cells expressing human CCR5; the gp120 glycoprotein of the adapted virus binds CCR5 directly, without prior interaction with CD4 |
PubMed
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env
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The chemokine receptor CCR5 is posttranslationally modified by sulfation of its N-terminal tyrosines; sulfated tyrosines contribute to the binding of CCR5 to MIP-1 alpha, MIP-1 beta, and HIV-1 gp120/CD4 complexes and to the ability of HIV-1 to enter cells |
PubMed
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env
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N-formyl-methionyl-leucylphenyl-alanine binding to formyl peptide receptor (FPR) results in significant attenuation of cell responses to CCR5 ligands and in inhibition of HIV-1 gp120-mediated fusion and infection of cells expressing CD4, CCR5, and FPR |
PubMed
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env
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HIV-1 gp120 from both CCR5- and CXCR4-tropic HIV-1 strains opens calcium-activated potassium (K(Ca)), chloride, and calcium-permeant nonselective cation channels in macrophages; these signals are mediated by CCR5 and CXCR4 |
PubMed
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env
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Anti-CCR5 monoclonal antibodies efficiently prevent HIV-1 infection by inducing receptor dimerization, but not by interfering with HIV-1 gp120 binding to CCR5 |
PubMed
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env
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Antibodies to specific epitopes of the CCR5 or CXCR4 chemokine receptors inhibit the entry of M-tropic, T-tropic, or dual-tropic HIV-1 into target cells by blocking the interaction of the receptors with the HIV-1 gp120/CD4 complex |
PubMed
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env
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AGP inhibits the binding of the HIV-1 gp120 consensus V3 domain (V3Cs) and macrophage inflammatory protein-1beta (MIP-1beta) to CCR5 on human monocyte-derived macrophages (MDM) |
PubMed
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env
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CCR5 and CXCR4 coreceptor engagement by HIV-1 gp120 in primary macrophages activates 2 members of the mitogen-activated protein kinase (MAPK) superfamily, c-Jun amino-terminal kinase and p38 MAPK |
PubMed
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env
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V1, V2, and V3 domains and N-linked glycosylation sites of HIV-1 gp120 confer coreceptor tropism; loss of an N-linked glycosylation site within V3 has a major influence on the virus switching from CCR5 to CXCR4 tropism in a V3 charge-dependent manner |
PubMed
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env
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HIV-1 gp120-induced PI3-kinase activity and calcium mobilization are inhibited by pertussis toxin and blocking antibodies directed against CCR5 and CXCR4, suggesting that this signaling is mediated through these chemokine receptors |
PubMed
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env
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HIV-1 gp120 interactions with CXCR4 and CCR5 lead to the cross-desensitization of CCR6 and CCR7; this gp120-induced inhibition is strictly dependent on CXCR4 or CCR5 and lipid rafts but not on CD4 or V(H)3-expressing BCR |
PubMed
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env
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Engagement of the CCR5 and CXCR4 receptors by HIV-1 gp120 induces tyrosine phosphorylation of the protein tyrosine kinase Pyk2 |
PubMed
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env
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The specific amino acids 298-329 in the V3 loop of HIV-1 gp120 that determine cellular tropism also regulate chemokine coreceptor (CCR5 or CXCR4) preference for cell entry by the virus |
PubMed
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env
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HIV-1-induced cell fusion is mediated by multiple regions within both the viral gp120 protein and the CCR5 coreceptor; dual-tropic virus isolates are less tolerant to changes in CCR5 than macrophage-tropic strains that have more restricted coreceptor use |
PubMed
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env
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Antibodies to specific epitopes of HIV-1 gp120 block the interaction of CCR5 with the gp120/CD4 complex, suggesting that a CD4-mediated conformational change in gp120 is required for subsequent binding to CCR5 |
PubMed
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env
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The HIV-1 envelope protein gp120 from macrophage-tropic HIV and SIV induces a signal through CCR5 on CD4+ T cells and macrophages, and this gp120-mediated signal transduction induces chemotaxis of T cells |
PubMed
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env
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The binding of HIV-1 gp120 to CCR5 and entry of macrophage-tropic HIV-1 isolates into cells is blocked by CCR5 antagonists or the chemokine RANTES, which interacts with CCR5 |
PubMed
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env
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The CCR5 chemokine receptor is required for the entry of macrophage-tropic HIV-1 into target cells; the HIV-1 gp120-CD4 complex binds CCR5, which inhibits the binding of the natural CCR5 ligands macrophage inflammatory protein (MIP)-1alpha and MIP-1beta |
PubMed
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Envelope transmembrane glycoprotein gp41
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env
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RANTES, MIP-1beta, and anti-CD4 antibodies inhibit CCR5-dependent cell-cell fusion mediated by HIV-1 gp120 and gp41 from macrophage-tropic isolates |
PubMed
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env
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HIV-1 gp120 and gp41 form a transitional complex with the CD4 receptor and CCR5/CXCR4 coreceptors during virus-cell and cell-cell membrane fusion |
PubMed
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env
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Secretion of IL-10 is upregulated by HIV-1 gp41 in monocytes through activation of cAMP/adenylate cyclase and p70 (S6)-kinase; up-regulation of IL-10 is paralleled by an enhanced expression of the chemokine receptor CCR5 |
PubMed
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env
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HIV-1 gp41 activates innate host immune cells through FPRL1, and the activation of FPRL1 by gp41 further induces the phosphorylation of the chemokine receptor CCR5 |
PubMed
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Nef
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nef
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SH3 (PxxP motif) and PACS (E4) interaction surfaces as well as the myristoylation site (G2) in HIV-1 Nef are required for Nef-mediated downregulation of CCR5 |
PubMed
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nef
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HIV-1 Nef downregulates cell-surface levels of CCR5 in CHO cells expressing human CCR5; the Nef-induced downregulation of CCR5 is as efficient as the downregulation induced by the natural beta-chemokine ligand RANTES |
PubMed
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Tat
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tat
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Results from the treatment of microglia with HIV-1 Tat suggest downregulation of CCR5 mRNA expression by HIV-1 Tat, however this was deemed to not be significant |
PubMed
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tat
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HIV-1 Tat upregulates CCR5 expression on monocytes/macrophages but not on lymphocytes, indicating a role for Tat in HIV-1 pathogenesis and in promoting the infection of monocytes/macrophages. |
PubMed
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tat
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HIV-1 Tat is associated with upregulation of CCR5 and MIP-1alpha expression in nodular lesions found in HIV encephalopathy and progressive multifocal leukoencephalopathy (PML), indicating a role for Tat in HIV-1 pathogenesis |
PubMed
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