Protein Arginine <i>N</i>-methyltransferases 5 and 7 Promote HIV-1 Production
Current therapies for human immunodeficiency virus type 1 (HIV-1) do not completely eliminate viral reservoirs in cells, such as macrophages. The HIV-1 accessory protein viral protein R (Vpr) promotes virus production in macrophages, and the maintenance of Vpr is essential for HIV-1 replication in t...
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doaj-7e4e09822885477a821d527d00cab2132020-11-25T02:10:43ZengMDPI AGViruses1999-49152020-03-0112335510.3390/v12030355v12030355Protein Arginine <i>N</i>-methyltransferases 5 and 7 Promote HIV-1 ProductionHironobu Murakami0Takehiro Suzuki1Kiyoto Tsuchiya2Hiroyuki Gatanaga3Manabu Taura4Eriko Kudo5Seiji Okada6Masami Takei7Kazumichi Kuroda8Tatsuo Yamamoto9Kyoji Hagiwara10Naoshi Dohmae11Yoko Aida12Viral Infectious Disease Unit, RIKEN, 2-1 Hirosawa, Wako, Saitama 351-0198, JapanBiomolecular Characterization Unit, RIKEN CSRS, 2-1 Hirosawa, Wako, Saitama 351-0198, JapanAIDS Clinical Center, National Center for Global Health and Medicine, 1-21-1 Toyama, Shinjuku-ku, Tokyo 162-8655, JapanAIDS Clinical Center, National Center for Global Health and Medicine, 1-21-1 Toyama, Shinjuku-ku, Tokyo 162-8655, JapanDivision of Hematopoiesis, Joint Research Center for Human Retrovirus Infection, Kumamoto University, 2-2-1 Honjo, Chuo-ku, Kumamoto 860-0811, JapanDivision of Hematopoiesis, Joint Research Center for Human Retrovirus Infection, Kumamoto University, 2-2-1 Honjo, Chuo-ku, Kumamoto 860-0811, JapanDivision of Hematopoiesis, Joint Research Center for Human Retrovirus Infection, Kumamoto University, 2-2-1 Honjo, Chuo-ku, Kumamoto 860-0811, JapanViral Infectious Disease Unit, RIKEN, 2-1 Hirosawa, Wako, Saitama 351-0198, JapanNihon University School of Medicine, 30-1 Oyaguchi, Itabashi, Tokyo 173-8610, JapanNihon University School of Medicine, 30-1 Oyaguchi, Itabashi, Tokyo 173-8610, JapanViral Infectious Disease Unit, RIKEN, 2-1 Hirosawa, Wako, Saitama 351-0198, JapanAIDS Clinical Center, National Center for Global Health and Medicine, 1-21-1 Toyama, Shinjuku-ku, Tokyo 162-8655, JapanViral Infectious Disease Unit, RIKEN, 2-1 Hirosawa, Wako, Saitama 351-0198, JapanCurrent therapies for human immunodeficiency virus type 1 (HIV-1) do not completely eliminate viral reservoirs in cells, such as macrophages. The HIV-1 accessory protein viral protein R (Vpr) promotes virus production in macrophages, and the maintenance of Vpr is essential for HIV-1 replication in these reservoir cells. We identified two novel Vpr-binding proteins, i.e., protein arginine <i>N</i>-methyltransferases (PRMTs) 5 and 7, using human monocyte-derived macrophages (MDMs). Both proteins found to be important for prevention of Vpr degradation by the proteasome; in the context of PRMT5 and PRMT7 knockdowns, degradation of Vpr could be prevented using a proteasome inhibitor. In MDMs infected with a wild-type strain, knockdown of PRMT5/PRMT7 and low expression of PRMT5 resulted in inefficient virus production like Vpr-deficient strain infections. Thus, our findings suggest that PRMT5 and PRMT7 support HIV-1 replication via maintenance of Vpr protein stability.https://www.mdpi.com/1999-4915/12/3/355hiv-1vprprmt5prmt7vpr-binding proteinvirus productionstabilitymacrophagepathogenesis |
collection |
DOAJ |
language |
English |
format |
Article |
sources |
DOAJ |
author |
Hironobu Murakami Takehiro Suzuki Kiyoto Tsuchiya Hiroyuki Gatanaga Manabu Taura Eriko Kudo Seiji Okada Masami Takei Kazumichi Kuroda Tatsuo Yamamoto Kyoji Hagiwara Naoshi Dohmae Yoko Aida |
spellingShingle |
Hironobu Murakami Takehiro Suzuki Kiyoto Tsuchiya Hiroyuki Gatanaga Manabu Taura Eriko Kudo Seiji Okada Masami Takei Kazumichi Kuroda Tatsuo Yamamoto Kyoji Hagiwara Naoshi Dohmae Yoko Aida Protein Arginine <i>N</i>-methyltransferases 5 and 7 Promote HIV-1 Production Viruses hiv-1 vpr prmt5 prmt7 vpr-binding protein virus production stability macrophage pathogenesis |
author_facet |
Hironobu Murakami Takehiro Suzuki Kiyoto Tsuchiya Hiroyuki Gatanaga Manabu Taura Eriko Kudo Seiji Okada Masami Takei Kazumichi Kuroda Tatsuo Yamamoto Kyoji Hagiwara Naoshi Dohmae Yoko Aida |
author_sort |
Hironobu Murakami |
title |
Protein Arginine <i>N</i>-methyltransferases 5 and 7 Promote HIV-1 Production |
title_short |
Protein Arginine <i>N</i>-methyltransferases 5 and 7 Promote HIV-1 Production |
title_full |
Protein Arginine <i>N</i>-methyltransferases 5 and 7 Promote HIV-1 Production |
title_fullStr |
Protein Arginine <i>N</i>-methyltransferases 5 and 7 Promote HIV-1 Production |
title_full_unstemmed |
Protein Arginine <i>N</i>-methyltransferases 5 and 7 Promote HIV-1 Production |
title_sort |
protein arginine <i>n</i>-methyltransferases 5 and 7 promote hiv-1 production |
publisher |
MDPI AG |
series |
Viruses |
issn |
1999-4915 |
publishDate |
2020-03-01 |
description |
Current therapies for human immunodeficiency virus type 1 (HIV-1) do not completely eliminate viral reservoirs in cells, such as macrophages. The HIV-1 accessory protein viral protein R (Vpr) promotes virus production in macrophages, and the maintenance of Vpr is essential for HIV-1 replication in these reservoir cells. We identified two novel Vpr-binding proteins, i.e., protein arginine <i>N</i>-methyltransferases (PRMTs) 5 and 7, using human monocyte-derived macrophages (MDMs). Both proteins found to be important for prevention of Vpr degradation by the proteasome; in the context of PRMT5 and PRMT7 knockdowns, degradation of Vpr could be prevented using a proteasome inhibitor. In MDMs infected with a wild-type strain, knockdown of PRMT5/PRMT7 and low expression of PRMT5 resulted in inefficient virus production like Vpr-deficient strain infections. Thus, our findings suggest that PRMT5 and PRMT7 support HIV-1 replication via maintenance of Vpr protein stability. |
topic |
hiv-1 vpr prmt5 prmt7 vpr-binding protein virus production stability macrophage pathogenesis |
url |
https://www.mdpi.com/1999-4915/12/3/355 |
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