HSF1 Activation Can Restrict HIV Replication
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...
| Main Authors: | , , , , , |
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| Format: | Article |
| Language: | English |
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American Chemical Society (ACS)
2021
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| Online Access: | https://hdl.handle.net/1721.1/135961 |
| _version_ | 1826206300806053888 |
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| author | Nekongo, Emmanuel E Ponomarenko, Anna I Dewal, Mahender B Butty, Vincent L Browne, Edward P Shoulders, Matthew D |
| author2 | Massachusetts Institute of Technology. Department of Chemistry |
| author_facet | Massachusetts Institute of Technology. Department of Chemistry Nekongo, Emmanuel E Ponomarenko, Anna I Dewal, Mahender B Butty, Vincent L Browne, Edward P Shoulders, Matthew D |
| author_sort | Nekongo, Emmanuel E |
| collection | MIT |
| description | 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. |
| first_indexed | 2024-09-23T13:27:17Z |
| format | Article |
| id | mit-1721.1/135961 |
| institution | Massachusetts Institute of Technology |
| language | English |
| last_indexed | 2024-09-23T13:27:17Z |
| publishDate | 2021 |
| publisher | American Chemical Society (ACS) |
| record_format | dspace |
| spelling | mit-1721.1/1359612023-02-23T20:49:22Z HSF1 Activation Can Restrict HIV Replication Nekongo, Emmanuel E Ponomarenko, Anna I Dewal, Mahender B Butty, Vincent L Browne, Edward P Shoulders, Matthew D Massachusetts Institute of Technology. Department of Chemistry 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. 2021-10-27T20:30:08Z 2021-10-27T20:30:08Z 2020 2021-07-14T17:53:12Z Article http://purl.org/eprint/type/JournalArticle https://hdl.handle.net/1721.1/135961 en 10.1021/ACSINFECDIS.0C00166 ACS Infectious Diseases Creative Commons Attribution-Noncommercial-Share Alike http://creativecommons.org/licenses/by-nc-sa/4.0/ application/pdf American Chemical Society (ACS) PMC |
| spellingShingle | Nekongo, Emmanuel E Ponomarenko, Anna I Dewal, Mahender B Butty, Vincent L Browne, Edward P Shoulders, Matthew D HSF1 Activation Can Restrict HIV Replication |
| title | HSF1 Activation Can Restrict HIV Replication |
| title_full | HSF1 Activation Can Restrict HIV Replication |
| title_fullStr | HSF1 Activation Can Restrict HIV Replication |
| title_full_unstemmed | HSF1 Activation Can Restrict HIV Replication |
| title_short | HSF1 Activation Can Restrict HIV Replication |
| title_sort | hsf1 activation can restrict hiv replication |
| url | https://hdl.handle.net/1721.1/135961 |
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