Crystal structure of the membrane (M) protein from a bat betacoronavirus

Author:

Wang Xiaodong1,Yang Yuwei1ORCID,Sun Ziyi1ORCID,Zhou Xiaoming1ORCID

Affiliation:

1. State Key Laboratory of Biotherapy, Department of Integrated Traditional Chinese and Western Medicine, Rare Diseases Center, West China Hospital, Sichuan University , Chengdu, Sichuan 610041 , China

Abstract

Abstract The membrane (M) protein is the most abundant structural protein of coronaviruses including MERS-CoV, SARS-CoV, and SARS-CoV-2, and plays a central role in virus assembly through its interaction with various partner proteins. However, mechanistic details about how M protein interacts with others remain elusive due to lack of high-resolution structures. Here, we present the first crystal structure of a betacoronavirus M protein from Pipistrellus bat coronavirus HKU5 (batCOV5-M), which is closely related to MERS-CoV, SARS-CoV, and SARS-CoV-2 M proteins. Furthermore, an interaction analysis indicates that the carboxy-terminus of the batCOV5 nucleocapsid (N) protein mediates its interaction with batCOV5-M. Combined with a computational docking analysis an M–N interaction model is proposed, providing insight into the mechanism of M protein–mediated protein interactions.

Funder

National Natural Science Foundation of China

Publisher

Oxford University Press (OUP)

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