期刊
NATURE COMMUNICATIONS
卷 13, 期 1, 页码 -出版社
NATURE PORTFOLIO
DOI: 10.1038/s41467-022-32019-3
关键词
-
资金
- Japanese Ministry of Education, Culture, Sports, Science, and Technology [20K15730, 22K15046, 19H03164, 22H02556, 19H00976, 21K19328]
- Program for Promoting Researches on the Supercomputer Fugaku (MD-driven Precision Medicine) [hp200129, hp210172]
- CREST, JST [JPMJCR21E4]
- Sumitomo Dainippon Pharma Co., Ltd.
- Takeda Science Foundation
- Mochida Memorial Foundation for Medical and Pharmaceutical Research
- Daiichi Sankyo Foundation of Life Science
- Naito Foundation
- Research Foundation for Pharmaceutical Sciences
- Basis for Supporting Innovative Drug Discovery and Life Science Research (BINDS) from the Japan Agency of Medical Research and Development (AMED) [JP21am0101115, 1570, 21am0101079, JP22ama121023, 1846, 1848]
- Research on Development of New Drugs from the AMED
- JST CREST [JPMJCR20HA]
- JSPS
- Joint Usage/Research Center program of Institute for Frontier Life and Medical Sciences Kyoto University
- Yokohama City University [SK202202]
- [18H05426]
M protein plays an essential role in the assembly and morphogenesis of SARS-CoV-2. The researchers found that M protein forms a mushroom-shaped dimer and further assembles into higher-order oligomers. The interaction of M protein with nucleocapsid protein and RNA suggests its role in the recruitment of these components during virus assembly.
M protein plays essential roles in virus assembly and morphogenesis. Here, authors reveal two cryo-EM structures of M protein from SARS-CoV-2 that suggest conformational dynamics of M protein and its role in virus assembly. The coronavirus membrane protein (M) is the most abundant viral structural protein and plays a central role in virus assembly and morphogenesis. However, the process of M protein-driven virus assembly are largely unknown. Here, we report the cryo-electron microscopy structure of the SARS-CoV-2 M protein in two different conformations. M protein forms a mushroom-shaped dimer, composed of two transmembrane domain-swapped three-helix bundles and two intravirion domains. M protein further assembles into higher-order oligomers. A highly conserved hinge region is key for conformational changes. The M protein dimer is unexpectedly similar to SARS-CoV-2 ORF3a, a viral ion channel. Moreover, the interaction analyses of M protein with nucleocapsid protein (N) and RNA suggest that the M protein mediates the concerted recruitment of these components through the positively charged intravirion domain. Our data shed light on the M protein-driven virus assembly mechanism and provide a structural basis for therapeutic intervention targeting M protein.
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