An unconventional topology of betacoronavirus membrane protein drives viral assembly

Science Bulletin, 16 June, 2025, DOI：https://doi.org/10.1016/j.scib.2025.06.012

An unconventional topology of betacoronavirus membrane protein drives viral assembly

Rui Lyu, Kaili Li, Lingjiao Xiang, Yingjian Li, Yaotian Liang, Xue Tan, Xiaoya Huang, Yu Chen, Hongyu Deng, Junjie Hu

Abstract

SARS-CoV-2 expresses four structural proteins, the membrane (M), envelope (E), spike (S), and nucleocapsid (N) proteins, along with a replicated viral genome, and delineates the process of viral assembly. S, E, and M are integral membrane proteins that are synthesized in the endoplasmic reticulum (ER), and N is cytosolic and escorts the viral genome for assembly. Based on findings for other betacoronaviruses, S/E/M have been proposed to meet in the ER-Golgi intermediate compartment (ERGIC), joined by N-genome, even though some assembled SARS-CoV-2 virions have been seen in the Golgi apparatus. The mechanism of SARS-CoV-2 assembly remains elusive.

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