Tyrosine 132 phosphorylation of influenza A virus M1 protein is crucial for virus replication by controlling the nuclear import of M1.

Abstract:

:Phosphorylation of viral proteins plays important roles in the influenza A virus (IAV) life cycle. By using mass spectrometry, we identified tyrosine 132 (Y132) as a phosphorylation site of the matrix protein (M1) of the influenza virus A/WSN/1933(H1N1). Phosphorylation at this site is essential to the process of virus replication by controlling the nuclear import of M1. We further demonstrated that the phosphorylated tyrosine is crucial for the binding of M1 to the nuclear import factor importin-α1, since any substitutions at this site severely reduce this protein-protein interaction and damage the importin-α1-mediated nuclear import of M1. Additionally, the tyrosine phosphorylation which leads to the nuclear import of M1 is blocked by a Janus kinase inhibitor. The present study reveals a pivotal role of this tyrosine phosphorylation in the intracellular transportation of M1, which controls the process of viral replication.

journal_name

J Virol

journal_title

Journal of virology

authors

Wang S,Zhao Z,Bi Y,Sun L,Liu X,Liu W

doi

10.1128/JVI.03024-12

subject

Has Abstract

pub_date

2013-06-01 00:00:00

pages

6182-91

issue

11

eissn

0022-538X

issn

1098-5514

pii

JVI.03024-12

journal_volume

87

pub_type

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