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-Structure paper
タイトル | Structure of SARS-CoV-2 membrane protein essential for virus assembly. |
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ジャーナル・号・ページ | Nat Commun, Vol. 13, Issue 1, Page 4399, Year 2022 |
掲載日 | 2022年8月5日 |
著者 | Zhikuan Zhang / Norimichi Nomura / Yukiko Muramoto / Toru Ekimoto / Tomoko Uemura / Kehong Liu / Moeko Yui / Nozomu Kono / Junken Aoki / Mitsunori Ikeguchi / Takeshi Noda / So Iwata / Umeharu Ohto / Toshiyuki Shimizu / |
PubMed 要旨 | 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 ...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. |
リンク | Nat Commun / PubMed:35931673 / PubMed Central |
手法 | EM (単粒子) |
解像度 | 2.7 - 6.2 Å |
構造データ | EMDB-31976: Cryo-EM reconstruction of SARS-CoV-2 M protein dimer in LMNG/CHS micelle EMDB-31977, PDB-7vgr: EMDB-31978, PDB-7vgs: |
由来 |
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キーワード | VIRAL PROTEIN/IMMUNE SYSTEM / SARS-CoV-2 / M protein / viral structural protein / virus assembly / VIRAL PROTEIN / VIRAL PROTEIN-IMMUNE SYSTEM complex |