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

Xiaodong Wang1, Yuwei Yang1, Ziyi Sun1

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

PNAS Nexus
|March 6, 2023
PubMed

Insights

Researchers determined the first high-resolution structure of a bat coronavirus M protein. This reveals how the M protein interacts with the N protein, crucial for coronavirus assembly.

Area of Science:

  • Virology
  • Structural Biology
  • Biochemistry

Background:

  • The membrane (M) protein is a key structural component of coronaviruses, essential for viral assembly.
  • Understanding M protein interactions is vital for deciphering coronavirus replication mechanisms.
  • High-resolution structural data for M proteins, particularly from betacoronaviruses, are limited.

Purpose of the Study:

  • To determine the first crystal structure of a betacoronavirus M protein.
  • To elucidate the interaction mechanism between the M protein and the nucleocapsid (N) protein.
  • To provide mechanistic insights into M protein-mediated interactions during coronavirus assembly.

Main Methods:

  • X-ray crystallography to obtain the high-resolution structure of bat coronavirus HKU5 M protein (batCOV5-M).
  • Protein interaction analysis to identify the binding interface between batCOV5-M and batCOV5 nucleocapsid (N) protein.
  • Computational docking analysis to model the M-N protein complex.

Main Results:

  • The first crystal structure of a betacoronavirus M protein (batCOV5-M) was determined.
  • The carboxy-terminus of the batCOV5 nucleocapsid (N) protein was identified as the mediator of interaction with batCOV5-M.
  • A structural model of the M-N protein interaction was proposed.

Conclusions:

  • The study provides crucial high-resolution structural information on a betacoronavirus M protein.
  • The findings reveal the specific interaction interface between M and N proteins, mediated by the N protein's C-terminus.
  • This work offers valuable insights into the molecular mechanisms underlying coronavirus assembly.
Keywords:
MERS-CoVSARS-CoVSARS-CoV-2X-ray crystallographyprotein interactionstructural protein

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