New structural insights into the multifunctional influenza A matrix protein 1

FEBS Letters

article

Julia Peukes¹  Xiaoli Xiong¹  John A. G. Briggs¹ 

[1] Structural Studies Division, Medical Research Council Laboratory of Molecular Biology;California Institute for Quantitative Biosciences ,(QB3), University of California;Bioland Laboratory ,(Guangzhou Regenerative Medicine and Health – Guangdong Laboratory), Guangzhou Institutes of Biomedicine and Health, Chinese Academy of Sciences;Department of Cell and Virus Structure, Max Planck Institute of Biochemistry

关键词: cryo-electron tomography;    enveloped virus;    helical reconstruction;    influenza virus;    M1;    matrix proteins;    protein oligomerization;    subtomogram averaging;    virus assembly;   

DOI  :  10.1002/1873-3468.14194

来源: John Wiley & Sons Ltd.

【 摘 要 】

Influenza A virus matrix protein 1 (M1) is the most abundant protein within virions and functions at multiple steps of the virus life cycle, including nuclear RNA export, virus particle assembly, and virus disassembly. Two recent publications have presented the first structures of full-length M1 and show that it assembles filaments in vitro via an interface between the N- and C-terminal domains of adjacent monomers. These filaments were found to be similar to those that form the endoskeleton of assembled virions. The structures provide a molecular basis to understand the functions of M1 during the virus life cycle. Here, we compare and discuss the two structures, and explore their implications for the mechanisms by which the multifunctional M1 protein can mediate virus assembly, interact with viral ribonucleoproteins and act during infection of a new cell.

【 授权许可】

Unknown