Structure of SARS-CoV-2 membrane protein essential for virus assembly

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 () and Toshiyuki Shimizu ()
Additional contact information
Zhikuan Zhang: The University of Tokyo
Norimichi Nomura: Kyoto University
Yukiko Muramoto: Kyoto University
Toru Ekimoto: Yokohama City University
Tomoko Uemura: Kyoto University
Kehong Liu: Kyoto University
Moeko Yui: The University of Tokyo
Nozomu Kono: The University of Tokyo
Junken Aoki: The University of Tokyo
Mitsunori Ikeguchi: Yokohama City University
Takeshi Noda: Kyoto University
So Iwata: Kyoto University
Umeharu Ohto: The University of Tokyo
Toshiyuki Shimizu: The University of Tokyo

Nature Communications, 2022, vol. 13, issue 1, 1-12

Abstract: Abstract 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.

Date: 2022
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Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:13:y:2022:i:1:d:10.1038_s41467-022-32019-3

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DOI: 10.1038/s41467-022-32019-3

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