Phosphorylation of influenza A virus NS1 protein at threonine 49 suppresses its interferon antagonistic activity.

ABSTRACT: Phosphorylation and dephosphorylation acts as a fundamental molecular switch that alters protein function and thereby regulates many cellular processes. The non-structural protein 1 (NS1) of influenza A virus is an important factor regulating virulence by counteracting cellular immune responses against viral infection. NS1 was shown to be phosphorylated at several sites; however, so far, no function has been conclusively assigned to these post-translational events yet. Here, we show that the newly identified phospho-site threonine 49 of NS1 is differentially phosphorylated in the viral replication cycle. Phosphorylation impairs binding of NS1 to double-stranded RNA and TRIM25 as well as complex formation with RIG-I, thereby switching off its interferon antagonistic activity. Because phosph

SUBMITTER: Kathum OA 

PROVIDER: S-EPMC5066752 | biostudies-literature | 2016 Jun

REPOSITORIES: biostudies-literature