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HSF1 Activation Can Restrict HIV Replication
- Source :
- PMC, ACS Infect Dis
- Publication Year :
- 2020
- Publisher :
- American Chemical Society (ACS), 2020.
-
Abstract
- Copyright © 2020 American Chemical Society. Host protein folding stress responses can play important roles in RNA virus replication and evolution. Prior work suggested a complicated interplay between the cytosolic proteostasis stress response, controlled by the transcriptional master regulator heat shock factor 1 (HSF1), and human immunodeficiency virus-1 (HIV-1). We sought to uncouple HSF1 transcription factor activity from cytotoxic proteostasis stress and thereby better elucidate the proposed role(s) of HSF1 in the HIV-1 lifecycle. To achieve this objective, we used chemical genetic, stress-independent control of HSF1 activity to establish whether and how HSF1 influences HIV-1 replication. Stress-independent HSF1 induction decreased both the total quantity and infectivity of HIV-1 virions. Moreover, HIV-1 was unable to escape HSF1-mediated restriction over the course of several serial passages. These results clarify the interplay between the host's heat shock response and HIV-1 infection and motivate continued investigation of chaperones as potential antiviral therapeutic targets.
- Subjects :
- 0301 basic medicine
Infectivity
biology
fungi
030106 microbiology
RNA virus
Virus Replication
biology.organism_classification
Article
Replication (computing)
Cell biology
03 medical and health sciences
Cytosol
030104 developmental biology
Infectious Diseases
Proteostasis
Heat Shock Transcription Factors
Humans
Cytotoxic T cell
Heat shock
HSF1
Heat-Shock Response
Molecular Chaperones
Subjects
Details
- ISSN :
- 23738227
- Volume :
- 6
- Database :
- OpenAIRE
- Journal :
- ACS Infectious Diseases
- Accession number :
- edsair.doi.dedup.....0c4cd115aa58a73346b5400f2ff3e4cc