SARS-CoV-2 membrane glycoprotein M antagonizes the MAVS-mediated innate antiviral response

A novel SARS-related coronavirus (SARS-CoV-2) has recently emerged as a serious pathogen that causes high morbidity and substantial mortality. However, the mechanisms by which SARS-CoV-2 evades host immunity remain poorly understood. Here, we identified SARS-CoV-2 membrane glycoprotein M as a negati...

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Published in	Cellular & molecular immunology Vol. 18; no. 3; pp. 613 - 620
Main Authors	Fu, Yu-Zhi, Wang, Su-Yun, Zheng, Zhou-Qin, Yi Huang, Li, Wei-Wei, Xu, Zhi-Sheng, Wang, Yan-Yi
Format	Journal Article
Language	English
Published	London Nature Publishing Group UK 01.03.2021 Nature Publishing Group
Subjects	631/250/2161 631/250/262 Adaptor Proteins, Signal Transducing - immunology Antibodies Antiviral drugs Biomedical and Life Sciences Biomedicine Coronaviruses COVID-19 - immunology Glycoproteins HEK293 Cells HeLa Cells Humans Immune response Immunity, Innate Immunology Innate immunity Interferon regulatory factor 3 M protein Medical Microbiology Microbiology Morbidity Proteins SARS-CoV-2 - immunology Severe acute respiratory syndrome coronavirus 2 Signal Transduction - immunology Vaccine Viral Matrix Proteins - immunology Innate immunity SARS-CoV-2 Membrane glycoprotein M MAVS Type I interferon
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Abstract	A novel SARS-related coronavirus (SARS-CoV-2) has recently emerged as a serious pathogen that causes high morbidity and substantial mortality. However, the mechanisms by which SARS-CoV-2 evades host immunity remain poorly understood. Here, we identified SARS-CoV-2 membrane glycoprotein M as a negative regulator of the innate immune response. We found that the M protein interacted with the central adaptor protein MAVS in the innate immune response pathways. This interaction impaired MAVS aggregation and its recruitment of downstream TRAF3, TBK1, and IRF3, leading to attenuation of the innate antiviral response. Our findings reveal a mechanism by which SARS-CoV-2 evades the innate immune response and suggest that the M protein of SARS-CoV-2 is a potential target for the development of SARS-CoV-2 interventions.
AbstractList	A novel SARS-related coronavirus (SARS-CoV-2) has recently emerged as a serious pathogen that causes high morbidity and substantial mortality. However, the mechanisms by which SARS-CoV-2 evades host immunity remain poorly understood. Here, we identified SARS-CoV-2 membrane glycoprotein M as a negative regulator of the innate immune response. We found that the M protein interacted with the central adaptor protein MAVS in the innate immune response pathways. This interaction impaired MAVS aggregation and its recruitment of downstream TRAF3, TBK1, and IRF3, leading to attenuation of the innate antiviral response. Our findings reveal a mechanism by which SARS-CoV-2 evades the innate immune response and suggest that the M protein of SARS-CoV-2 is a potential target for the development of SARS-CoV-2 interventions.A novel SARS-related coronavirus (SARS-CoV-2) has recently emerged as a serious pathogen that causes high morbidity and substantial mortality. However, the mechanisms by which SARS-CoV-2 evades host immunity remain poorly understood. Here, we identified SARS-CoV-2 membrane glycoprotein M as a negative regulator of the innate immune response. We found that the M protein interacted with the central adaptor protein MAVS in the innate immune response pathways. This interaction impaired MAVS aggregation and its recruitment of downstream TRAF3, TBK1, and IRF3, leading to attenuation of the innate antiviral response. Our findings reveal a mechanism by which SARS-CoV-2 evades the innate immune response and suggest that the M protein of SARS-CoV-2 is a potential target for the development of SARS-CoV-2 interventions. A novel SARS-related coronavirus (SARS-CoV-2) has recently emerged as a serious pathogen that causes high morbidity and substantial mortality. However, the mechanisms by which SARS-CoV-2 evades host immunity remain poorly understood. Here, we identified SARS-CoV-2 membrane glycoprotein M as a negative regulator of the innate immune response. We found that the M protein interacted with the central adaptor protein MAVS in the innate immune response pathways. This interaction impaired MAVS aggregation and its recruitment of downstream TRAF3, TBK1, and IRF3, leading to attenuation of the innate antiviral response. Our findings reveal a mechanism by which SARS-CoV-2 evades the innate immune response and suggest that the M protein of SARS-CoV-2 is a potential target for the development of SARS-CoV-2 interventions.
Author	Fu, Yu-Zhi Yi Huang Zheng, Zhou-Qin Li, Wei-Wei Wang, Su-Yun Wang, Yan-Yi Xu, Zhi-Sheng
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Snippet	A novel SARS-related coronavirus (SARS-CoV-2) has recently emerged as a serious pathogen that causes high morbidity and substantial mortality. However, the...
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SubjectTerms	631/250/2161 631/250/262 Adaptor Proteins, Signal Transducing - immunology Antibodies Antiviral drugs Biomedical and Life Sciences Biomedicine Coronaviruses COVID-19 - immunology Glycoproteins HEK293 Cells HeLa Cells Humans Immune response Immunity, Innate Immunology Innate immunity Interferon regulatory factor 3 M protein Medical Microbiology Microbiology Morbidity Proteins SARS-CoV-2 - immunology Severe acute respiratory syndrome coronavirus 2 Signal Transduction - immunology Vaccine Viral Matrix Proteins - immunology
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Title	SARS-CoV-2 membrane glycoprotein M antagonizes the MAVS-mediated innate antiviral response
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