tetano
Editor, Senior Moderator
Nat Commun
. 2022 Aug 5;13(1):4399.
doi: 10.1038/s41467-022-32019-3.
Structure of SARS-CoV-2 membrane protein essential for virus assembly
Zhikuan Zhang[SUP] 1 [/SUP], Norimichi Nomura[SUP] 2 [/SUP], Yukiko Muramoto[SUP] 3 4 5 [/SUP], Toru Ekimoto[SUP] 6 [/SUP], Tomoko Uemura[SUP] 2 [/SUP], Kehong Liu[SUP] 2 [/SUP], Moeko Yui[SUP] 1 [/SUP], Nozomu Kono[SUP] 1 [/SUP], Junken Aoki[SUP] 1 [/SUP], Mitsunori Ikeguchi[SUP] 6 7 [/SUP], Takeshi Noda[SUP] 3 4 5 [/SUP], So Iwata[SUP] 2 8 [/SUP], Umeharu Ohto[SUP] 9 [/SUP], Toshiyuki Shimizu[SUP] 10 [/SUP]
Affiliations
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.
. 2022 Aug 5;13(1):4399.
doi: 10.1038/s41467-022-32019-3.
Structure of SARS-CoV-2 membrane protein essential for virus assembly
Zhikuan Zhang[SUP] 1 [/SUP], Norimichi Nomura[SUP] 2 [/SUP], Yukiko Muramoto[SUP] 3 4 5 [/SUP], Toru Ekimoto[SUP] 6 [/SUP], Tomoko Uemura[SUP] 2 [/SUP], Kehong Liu[SUP] 2 [/SUP], Moeko Yui[SUP] 1 [/SUP], Nozomu Kono[SUP] 1 [/SUP], Junken Aoki[SUP] 1 [/SUP], Mitsunori Ikeguchi[SUP] 6 7 [/SUP], Takeshi Noda[SUP] 3 4 5 [/SUP], So Iwata[SUP] 2 8 [/SUP], Umeharu Ohto[SUP] 9 [/SUP], Toshiyuki Shimizu[SUP] 10 [/SUP]
Affiliations
- PMID: 35931673
- DOI: 10.1038/s41467-022-32019-3
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.