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The molecular architecture of the SARS-CoV-2 double-membrane vesicle (DMV) pore complex, a crucial component in coronavirus replication, has been unveiled in a study by Huang et al.

Using cryogenic electron tomography and subtomogram averaging, the researchers resolved the structure of the nsp3-nsp4 pore complex at 4.2 Å resolution. The complex consists of 12 copies each of nsp3 and nsp4, organized in 4 concentric stacking hexamer rings, mimicking a miniature nuclear pore complex.

The study demonstrates that positively charged residues at the constriction sites are critical for virus replication, potentially mediating metabolites and RNA transport. This research provides a groundwork to understand DMV pore formation and RNA translocation in the Coronaviridae family, potentially extending to other viruses in the Arteviridae family of Nidovirale.

An IonOpticks Aurora Ultimate 25×75 C18 UHPLC column was used for chromatographic separation in the mass spectrometry analysis.

Publication
Nature

Authors

Yixin Huang, Tongyun Wang, Lijie Zhong, Wenxin Zhang, Yu Zhang, Xiulian Yu, Shuofeng Yuan, Tao Ni

Title

Molecular architecture of coronavirus double-membrane vesicle pore complex