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Chaudhary P, P. and Khan S, S. and Rawat P, P. and Augustine , T and Raynes , D.A. and Mitra , D. (2015) HSP70 binding protein 1 (HspBP1) suppresses HIV-1 replication by inhibiting NF-�B mediated activation of viral gene expression. Nucleic Acids Research. doi: 10.1093/nar/gkv1151.

69. Dr. Mitra D. (Nucl. Acid Res.) paid open access.pdf

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HIV-1 efficiently hijacks host cellular machinery and exploits a plethora of host–viral interactions for its successful survival. Identifying host factors that affect susceptibility or resistance to HIV-1 may offer a promising therapeutic strategy against HIV-1. Previously, we have reported that heat shock proteins, HSP40 and HSP70 reciprocally regulate HIV-1 geneexpression and replication. In the present study, we have identified HSP70 binding protein 1 (HspBP1) as a host-intrinsic inhibitor of HIV-1. HspBP1 level was found to be significantly down modulated during HIV- 1 infection and virus production inversely co-related with HspBP1 expression. Our results further demonstrate that HspBP1 inhibits HIV-1 long terminal repeat (LTR) promoter activity. Gel shift and chromatin immunoprecipitation assays revealed that HspBP1 was recruited on HIV-1 LTR at NF-�B enhancer region (�B sites). The binding of HspBP1 to �B sites obliterates the binding of NF-�B hetero-dimer (p50/p65) to the same region, leading to repression in NF-�B mediated activation of LTR-driven gene-expression. HspBP1 also plays an inhibitory role in the reactivation of latently infected cells, corroborating its repressive effect on NF-�B pathway. Thus, our results clearly show that HspBP1 acts as an endogenous negative regulator of HIV-1 gene-expression and replication by suppressing NF-�B-mediated activation of viral transcription.

Item Type: Article
Additional Information: This is open access article for full text click above weblink
Subjects: Cell Biology
Depositing User: Mr. Rameshwar Nema
Date Deposited: 22 Dec 2015 05:40
Last Modified: 19 Feb 2016 03:31
URI: http://nccs.sciencecentral.in/id/eprint/222

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