ArticleThe Journal of biological chemistry2011
Impaired infectivity of ritonavir-resistant HIV is rescued by heat shock protein 90AB1.
Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
16 citing papers in PubMed, 26 citations in OpenAlex.
- HIV and the gut: implications for HIV persistence, immune dysfunction and cure strategies.Frontiers in immunology · 2025Review
- The immune-evasive proline-283 substitution in influenza nucleoprotein increases aggregation propensity without altering the native structure.Science advances · 2024Article
- HIV Reservoirs and Treatment Strategies toward Curing HIV Infection.International journal of molecular sciences · 2024Review
- Viral Evolution Shaped by Host Proteostasis Networks.Annual review of virology · 2023Review
- Article
- Review
- Diversity in heat shock protein families: functional implications in virus infection with a comprehensive insight of their role in the HIV-1 life cycle.Cell stress & chaperones · 2021Review
- Block-And-Lock: New Horizons for a Cure for HIV-1.Viruses · 2020Review
- Marine medaka heat shock protein 90ab1 is a receptor for red-spotted grouper nervous necrosis virus and promotes virus internalization through clathrin-mediated endocytosis.PLoS pathogens · 2020Article
- Block-And-Lock Strategies to Cure HIV Infection.Viruses · 2020Review
- Inhibition of Heat Shock Protein 90 Prevents HIV Rebound.The Journal of biological chemistry · 2016Article
- HSP90AB1: Helping the good and the bad.Gene · 2016Review
- On-chip Extraction of Intracellular Molecules in White Blood Cells from Whole Blood.Scientific reports · 2015Article
- The conserved set of host proteins incorporated into HIV-1 virions suggests a common egress pathway in multiple cell types.Journal of proteome research · 2013Article
- Heat shock protein 90AB1 and hyperthermia rescue infectivity of HIV with defective cores.Virology · 2013Article
- Hyperthermia stimulates HIV-1 replication.PLoS pathogens · 2012Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Certain ritonavir resistance mutations impair HIV infectivity through incomplete Gag processing by the mutant viral protease. Analysis of the mutant virus phenotype indicates that accumulation of capsid-spacer peptide 1 precursor protein in virus particles impairs HIV infectivity and that the protease mutant virus is arrested during the early postentry stage of HIV infection before proviral DNA synthesis. However, activation of the target cell can rescue this defect, implying that specific host factors expressed in activated cells can compensate for the defect in ritonavir-resistant HIV. This ability to rescue impaired HIV replication presented a unique opportunity to identify host factors involved in postentry HIV replication, and we designed a functional genetic screen so that expression of a given host factor extracted from activated T cells would lead directly to its discovery by rescuing mutant virus replication in nonactivated T cells. We identified the cellular heat shock protein 90 kDa α (cytosolic), class B member 1 (HSP90AB1) as a host factor that can rescue impaired replication of ritonavir-resistant HIV. Moreover, we show that pharmacologic inhibition of HSP90AB1 with 17-(allylamino)-17-demethoxygeldanamycin (tanespimycin) has potent in vitro anti-HIV activity and that ritonavir-resistant HIV is hypersensitive to the drug. These results suggest a possible role for HSP90AB1 in postentry HIV replication and may provide an attractive target for therapeutic intervention.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.