Envelope surface glycoprotein gp120
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env
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HIV-1 Env gp120 upregulates HSPA5 (GRP78/BiP) in SVGA cells and human fetal astrocytes |
PubMed
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env
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Tandem affinity purification and mass spectrometry analysis identify heat shock 70kDa protein 5 (HSPA5; 78kDa glucose-regulated protein), HIV-1 Gag, Gag/Pol, gp120, and Nef incorporated into staufen1 RNP complexes isolated from HIV-1-expressing cells |
PubMed
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env
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Over expression of hsp70 with a herpes viral amplicon vector protects cultured hippocampal rat neurons from gp120 neurotoxicity |
PubMed
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env
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The exposure of permissive CD4+ cells to HIV-1 gp120 increases the synthesis and nuclear translocation of 70kDa heat shock protein |
PubMed
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Envelope surface glycoprotein gp160, precursor
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env
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HIV-1 gp160 interacts with HSPA5; predicted interaction to be within the endoplasmic reticulum and function as chaperone for endoplasmic reticulum-associated degradation |
PubMed
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env
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Newly synthesized HIV-1 gp160 interacts with GRP78-BiP in pulse-chase experiments; the interaction sites of gp160 with BiP include residues 115-132, 484-490, 602-616, 676-690, and 776-807 |
PubMed
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Gag-Pol
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gag-pol
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Tandem affinity purification and mass spectrometry analysis identify heat shock 70kDa protein 5 (HSPA5; 78kDa glucose-regulated protein), HIV-1 Gag, Gag/Pol, gp120, and Nef incorporated into staufen1 RNP complexes isolated from HIV-1-expressing cells |
PubMed
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Nef
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nef
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Tandem affinity purification and mass spectrometry analysis identify heat shock 70kDa protein 5 (HSPA5; 78kDa glucose-regulated protein), HIV-1 Gag, Gag/Pol, gp120, and Nef incorporated into staufen1 RNP complexes isolated from HIV-1-expressing cells |
PubMed
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nef
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Heat shock proteins Hsp40 and Hsp70 interact with HIV-1 Nef and form a complex in cells |
PubMed
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Pr55(Gag)
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gag
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Tandem affinity purification and mass spectrometry analysis identify heat shock 70kDa protein 5 (HSPA5; 78kDa glucose-regulated protein), HIV-1 Gag, Gag/Pol, gp120, and Nef incorporated into staufen1 RNP complexes isolated from HIV-1-expressing cells |
PubMed
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gag
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Hsp70 is incorporated into HIV-1 virions through an interaction with HIV-1 Gag |
PubMed
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gag
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Hsp70 co-sediments with HIV-1 capsid protein in sucrose density gradients, providing evidence that it is specifically incorporated into HIV-1 virions through an interaction with HIV-1 Gag proteins |
PubMed
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Tat
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tat
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Exposure of human umbilical vein endothelial cells to HIV-1 Tat causes broad activation of the unfolded-protein response in ER with phosphorylation of PERK, eIF2alpha, and JNK and induction of Grp78/BiP |
PubMed
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tat
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Hsp70 and Hsp90 and Cdc37 regulate the stabilization and folding of CDK9 as well as the assembly of an active CDK9/cyclin T1 complex responsible for P-TEFb-mediated HIV-1 Tat transactivation |
PubMed
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Vpr
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vpr
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A stable-isotope labeling by amino acids in cell culture coupled with mass spectrometry-based proteomics identifies upregulation of heat shock 70kDa protein 5 (HSPA5, GRP78) expression by HIV-1 Vpr in Vpr transduced macrophages |
PubMed
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vpr
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HIV-1 Vpr is required for the inhibitory effect of Hsp70 on viral gene expression and replication |
PubMed
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vpr
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HIV-1 Vpr significantly increases expression level of GRP78 in the endoplasmic reticulum |
PubMed
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vpr
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HIV-1 Vpr competes with Hsp70 for binding to karyopherin alpha |
PubMed
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matrix
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gag
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Hsp70 facilitates nuclear import of HIV-1 preintegration complexes by stimulating the binding of HIV-1 Matrix to karyopherin alpha |
PubMed
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