Viral Hijacking of BET Proteins
Proteins of the bromodomain and exterminal domain (BET) family mediate critical host functions such as cell proliferation, transcriptional regulation, and the innate immune response, which makes them preferred targets for viruses. These multidomain proteins are best known as transcriptional effector...
| Main Authors: | , |
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| Format: | Article |
| Language: | English |
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MDPI AG
2022-10-01
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| Series: | Viruses |
| Subjects: | |
| Online Access: | https://www.mdpi.com/1999-4915/14/10/2274 |
| _version_ | 1827647676333686784 |
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| author | Irene P. Chen Melanie Ott |
| author_facet | Irene P. Chen Melanie Ott |
| author_sort | Irene P. Chen |
| collection | DOAJ |
| description | Proteins of the bromodomain and exterminal domain (BET) family mediate critical host functions such as cell proliferation, transcriptional regulation, and the innate immune response, which makes them preferred targets for viruses. These multidomain proteins are best known as transcriptional effectors able to read acetylated histone and non-histone proteins through their tandem bromodomains. They also contain other short motif-binding domains such as the extraterminal domain, which recognizes transcriptional regulatory proteins. Here, we describe how different viruses have evolved to hijack or disrupt host BET protein function through direct interactions with BET family members to support their own propagation. The network of virus-BET interactions emerges as highly intricate, which may complicate the use of small-molecule BET inhibitors–currently in clinical development for the treatment of cancer and cardiovascular diseases–to treat viral infections. |
| first_indexed | 2024-03-09T19:23:03Z |
| format | Article |
| id | doaj.art-901ed41f9b1440408a75fc7b1589d4c2 |
| institution | Directory Open Access Journal |
| issn | 1999-4915 |
| language | English |
| last_indexed | 2024-03-09T19:23:03Z |
| publishDate | 2022-10-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Viruses |
| spelling | doaj.art-901ed41f9b1440408a75fc7b1589d4c22023-11-24T03:10:36ZengMDPI AGViruses1999-49152022-10-011410227410.3390/v14102274Viral Hijacking of BET ProteinsIrene P. Chen0Melanie Ott1Gladstone Institutes, San Francisco, CA 94158, USAGladstone Institutes, San Francisco, CA 94158, USAProteins of the bromodomain and exterminal domain (BET) family mediate critical host functions such as cell proliferation, transcriptional regulation, and the innate immune response, which makes them preferred targets for viruses. These multidomain proteins are best known as transcriptional effectors able to read acetylated histone and non-histone proteins through their tandem bromodomains. They also contain other short motif-binding domains such as the extraterminal domain, which recognizes transcriptional regulatory proteins. Here, we describe how different viruses have evolved to hijack or disrupt host BET protein function through direct interactions with BET family members to support their own propagation. The network of virus-BET interactions emerges as highly intricate, which may complicate the use of small-molecule BET inhibitors–currently in clinical development for the treatment of cancer and cardiovascular diseases–to treat viral infections.https://www.mdpi.com/1999-4915/14/10/2274CoronavirusFlavivirusPapillomavirusPolyomavirusRetrovirusHerpesvirus |
| spellingShingle | Irene P. Chen Melanie Ott Viral Hijacking of BET Proteins Viruses Coronavirus Flavivirus Papillomavirus Polyomavirus Retrovirus Herpesvirus |
| title | Viral Hijacking of BET Proteins |
| title_full | Viral Hijacking of BET Proteins |
| title_fullStr | Viral Hijacking of BET Proteins |
| title_full_unstemmed | Viral Hijacking of BET Proteins |
| title_short | Viral Hijacking of BET Proteins |
| title_sort | viral hijacking of bet proteins |
| topic | Coronavirus Flavivirus Papillomavirus Polyomavirus Retrovirus Herpesvirus |
| url | https://www.mdpi.com/1999-4915/14/10/2274 |
| work_keys_str_mv | AT irenepchen viralhijackingofbetproteins AT melanieott viralhijackingofbetproteins |