tetano
Editor, Senior Moderator
ell Microbiol. 2015 Dec 21. doi: 10.1111/cmi.12559. [Epub ahead of print] [h=1]Phosphorylation of Influenza A virus NS1 protein at threonine 49 suppresses its interferon antagonistic activity.[/h] Kathum OA[SUP]1[/SUP], Schr?der T[SUP]1[/SUP], Anhlan D[SUP]1[/SUP], Nordhoff C[SUP]1[/SUP], Liedmann S[SUP]1[/SUP], Pande A[SUP]2,[/SUP][SUP]3[/SUP], Mellmann A[SUP]4[/SUP], Ehrhardt C[SUP]1[/SUP], Wixler V[SUP]1[/SUP], Ludwig S[SUP]1[/SUP].
[h=3]Author information[/h]
[h=3]Abstract[/h] 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 this 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 dsRNA and TRIM25 as well as complex formation with RIG-I thereby switching-off its interferon antagonistic activity. Because phosphorylation was shown to occur at later stages of infection, we hypothesize that at this stage other functions of the multifunctional NS1 beyond its IFN antagonistic activity are needed. This article is protected by copyright. All rights reserved.
This article is protected by copyright. All rights reserved.
PMID: 26687707 [PubMed - as supplied by publisher]
[h=3]Author information[/h]
[h=3]Abstract[/h] 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 this 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 dsRNA and TRIM25 as well as complex formation with RIG-I thereby switching-off its interferon antagonistic activity. Because phosphorylation was shown to occur at later stages of infection, we hypothesize that at this stage other functions of the multifunctional NS1 beyond its IFN antagonistic activity are needed. This article is protected by copyright. All rights reserved.
This article is protected by copyright. All rights reserved.
PMID: 26687707 [PubMed - as supplied by publisher]