MARCH8 Restricts RSV Replication by Promoting Cellular Apoptosis Through Ubiquitin-Mediated Proteolysis of Viral SH Protein

Numerous host factors function as intrinsic antiviral effectors to attenuate viral replication. MARCH8 is an E3 ubiquitin ligase that has been identified as a host restriction factor that inhibits the replication of various viruses. This study elucidated the mechanism by which MARCH8 restricts respi...

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Published inViruses Vol. 16; no. 12; p. 1935
Main Authors Okura, Takashi, Takahashi, Tatsuki, Kameya, Taichi, Mizukoshi, Fuminori, Nakai, Yusuke, Kakizaki, Masatoshi, Nishi, Mayuko, Otsuki, Noriyuki, Kimura, Hirokazu, Miyakawa, Kei, Shirato, Kazuya, Kamitani, Wataru, Ryo, Akihide
Format Journal Article
LanguageEnglish
Published Switzerland MDPI AG 01.12.2024
MDPI
Subjects
A549 Cells
Antibodies
Antiviral drugs
Apoptosis
Cell Line
Cell survival
Cloning
Control
Degradation
Disease transmission
Genomes
Health aspects
HEK293 Cells
Host-Pathogen Interactions
Humans
Hydrophobicity
Influenza
MARCH8
Physiological aspects
Plasmids
Protein expression
Proteins
Proteolysis
Replication
Respiratory syncytial virus
Respiratory Syncytial Virus Infections - metabolism
Respiratory Syncytial Virus Infections - virology
Respiratory Syncytial Virus, Human - genetics
Respiratory Syncytial Virus, Human - metabolism
Respiratory Syncytial Virus, Human - physiology
small hydrophobic protein
Ubiquitin
Ubiquitin - metabolism
Ubiquitin-protein ligase
Ubiquitin-Protein Ligases - genetics
Ubiquitin-Protein Ligases - metabolism
Ubiquitination
Vaccines
Viral infections
Viral Proteins - genetics
Viral Proteins - metabolism
Virus Replication
Viruses
Japan
United States > US
apoptosis
MARCH8
ubiquitination
respiratory syncytial virus
small hydrophobic protein
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Abstract Numerous host factors function as intrinsic antiviral effectors to attenuate viral replication. MARCH8 is an E3 ubiquitin ligase that has been identified as a host restriction factor that inhibits the replication of various viruses. This study elucidated the mechanism by which MARCH8 restricts respiratory syncytial virus (RSV) replication through selective degradation of the viral small hydrophobic (SH) protein. We demonstrated that MARCH8 directly interacts with RSV-SH and catalyzes its ubiquitination at lysine 13, leading to SH degradation via the ubiquitin-lysosomal pathway. Functionally, MARCH8 expression enhances RSV-induced apoptosis through SH degradation, ultimately reducing viral titers. Conversely, an RSV strain harboring the SH-K13R mutation exhibited prolonged SH protein stability and attenuated apoptosis in infected cells, even in the presence of MARCH8. Targeted depletion of MARCH8 enhances cellular survival and potentially increases viral persistence. These findings demonstrate that MARCH8 promotes the early elimination of virus-infected cells by abrogating the anti-apoptotic function of SH, thereby reducing viral transmission. Our study provides novel insights into the interplay between host restriction factors and viral evasion strategies, potentially providing new therapeutic approaches for RSV infections.
AbstractList Numerous host factors function as intrinsic antiviral effectors to attenuate viral replication. MARCH8 is an E3 ubiquitin ligase that has been identified as a host restriction factor that inhibits the replication of various viruses. This study elucidated the mechanism by which MARCH8 restricts respiratory syncytial virus (RSV) replication through selective degradation of the viral small hydrophobic (SH) protein. We demonstrated that MARCH8 directly interacts with RSV-SH and catalyzes its ubiquitination at lysine 13, leading to SH degradation via the ubiquitin-lysosomal pathway. Functionally, MARCH8 expression enhances RSV-induced apoptosis through SH degradation, ultimately reducing viral titers. Conversely, an RSV strain harboring the SH-K13R mutation exhibited prolonged SH protein stability and attenuated apoptosis in infected cells, even in the presence of MARCH8. Targeted depletion of MARCH8 enhances cellular survival and potentially increases viral persistence. These findings demonstrate that MARCH8 promotes the early elimination of virus-infected cells by abrogating the anti-apoptotic function of SH, thereby reducing viral transmission. Our study provides novel insights into the interplay between host restriction factors and viral evasion strategies, potentially providing new therapeutic approaches for RSV infections.
Numerous host factors function as intrinsic antiviral effectors to attenuate viral replication. MARCH8 is an E3 ubiquitin ligase that has been identified as a host restriction factor that inhibits the replication of various viruses. This study elucidated the mechanism by which MARCH8 restricts respiratory syncytial virus (RSV) replication through selective degradation of the viral small hydrophobic (SH) protein. We demonstrated that MARCH8 directly interacts with RSV-SH and catalyzes its ubiquitination at lysine 13, leading to SH degradation via the ubiquitin-lysosomal pathway. Functionally, MARCH8 expression enhances RSV-induced apoptosis through SH degradation, ultimately reducing viral titers. Conversely, an RSV strain harboring the SH-K13R mutation exhibited prolonged SH protein stability and attenuated apoptosis in infected cells, even in the presence of MARCH8. Targeted depletion of MARCH8 enhances cellular survival and potentially increases viral persistence. These findings demonstrate that MARCH8 promotes the early elimination of virus-infected cells by abrogating the anti-apoptotic function of SH, thereby reducing viral transmission. Our study provides novel insights into the interplay between host restriction factors and viral evasion strategies, potentially providing new therapeutic approaches for RSV infections.Numerous host factors function as intrinsic antiviral effectors to attenuate viral replication. MARCH8 is an E3 ubiquitin ligase that has been identified as a host restriction factor that inhibits the replication of various viruses. This study elucidated the mechanism by which MARCH8 restricts respiratory syncytial virus (RSV) replication through selective degradation of the viral small hydrophobic (SH) protein. We demonstrated that MARCH8 directly interacts with RSV-SH and catalyzes its ubiquitination at lysine 13, leading to SH degradation via the ubiquitin-lysosomal pathway. Functionally, MARCH8 expression enhances RSV-induced apoptosis through SH degradation, ultimately reducing viral titers. Conversely, an RSV strain harboring the SH-K13R mutation exhibited prolonged SH protein stability and attenuated apoptosis in infected cells, even in the presence of MARCH8. Targeted depletion of MARCH8 enhances cellular survival and potentially increases viral persistence. These findings demonstrate that MARCH8 promotes the early elimination of virus-infected cells by abrogating the anti-apoptotic function of SH, thereby reducing viral transmission. Our study provides novel insights into the interplay between host restriction factors and viral evasion strategies, potentially providing new therapeutic approaches for RSV infections.
Audience Academic
Author Ryo, Akihide
Takahashi, Tatsuki
Kakizaki, Masatoshi
Okura, Takashi
Mizukoshi, Fuminori
Otsuki, Noriyuki
Kimura, Hirokazu
Kameya, Taichi
Miyakawa, Kei
Shirato, Kazuya
Nakai, Yusuke
Kamitani, Wataru
Nishi, Mayuko
AuthorAffiliation 3 Life Science Laboratory, Technology and Development Division, Kanto Chemical Co., Inc., Chuo-ku 259-1146, Kanagawa, Japan
1 Department of Virology 3, National Institute of Infectious Diseases, Musashimurayama 208-0011, Tokyo, Japan; t-okura@niid.go.jp (T.O.); t-kameya@niid.go.jp (T.K.); mzksh@niid.go.jp (F.M.); yusuke06@niid.go.jp (Y.N.); kakizaki@niid.go.jp (M.K.); mnishi@niid.go.jp (M.N.); otsuki@niid.go.jp (N.O.); shirato@niid.go.jp (K.S.)
2 Department of Infectious Diseases and Host Defense, Graduate School of Medicine, Gunma University, Maebashi 371-8511, Gunma, Japan; ta-takahashi@gunma-u.ac.jp (T.T.); wakamita@gunma-u.ac.jp (W.K.)
4 Department of Health Science, Graduate School of Health Sciences, Gunma Paz University, Takasaki 370-0006, Gunma, Japan; h-kimura@paz.ac.jp
5 Research Center for Influenza and Respiratory Viruses, National Institute of Infectious Diseases, Musashimurayama 208-0011, Tokyo, Japan; keim@niid.go.jp
6 Department of Microbiology, Graduate School of Medicine,
AuthorAffiliation_xml – name: 4 Department of Health Science, Graduate School of Health Sciences, Gunma Paz University, Takasaki 370-0006, Gunma, Japan; h-kimura@paz.ac.jp
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– name: 2 Department of Infectious Diseases and Host Defense, Graduate School of Medicine, Gunma University, Maebashi 371-8511, Gunma, Japan; ta-takahashi@gunma-u.ac.jp (T.T.); wakamita@gunma-u.ac.jp (W.K.)
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Keywords apoptosis
MARCH8
ubiquitination
respiratory syncytial virus
small hydrophobic protein
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Snippet Numerous host factors function as intrinsic antiviral effectors to attenuate viral replication. MARCH8 is an E3 ubiquitin ligase that has been identified as a...
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SubjectTerms A549 Cells
Antibodies
Antiviral drugs
Apoptosis
Cell Line
Cell survival
Cloning
Control
Degradation
Disease transmission
Genomes
Health aspects
HEK293 Cells
Host-Pathogen Interactions
Humans
Hydrophobicity
Influenza
MARCH8
Physiological aspects
Plasmids
Protein expression
Proteins
Proteolysis
Replication
Respiratory syncytial virus
Respiratory Syncytial Virus Infections - metabolism
Respiratory Syncytial Virus Infections - virology
Respiratory Syncytial Virus, Human - genetics
Respiratory Syncytial Virus, Human - metabolism
Respiratory Syncytial Virus, Human - physiology
small hydrophobic protein
Ubiquitin
Ubiquitin - metabolism
Ubiquitin-protein ligase
Ubiquitin-Protein Ligases - genetics
Ubiquitin-Protein Ligases - metabolism
Ubiquitination
Vaccines
Viral infections
Viral Proteins - genetics
Viral Proteins - metabolism
Virus Replication
Viruses
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Title MARCH8 Restricts RSV Replication by Promoting Cellular Apoptosis Through Ubiquitin-Mediated Proteolysis of Viral SH Protein
URI https://www.ncbi.nlm.nih.gov/pubmed/39772241
https://www.proquest.com/docview/3149764972
https://www.proquest.com/docview/3153872524
https://pubmed.ncbi.nlm.nih.gov/PMC11680241
https://doaj.org/article/0145bd505d1948cd867f7dc5c93e4bc4
Volume 16
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