tetano
Editor, Senior Moderator
J Gen Virol. 2017 Sep 4. doi: 10.1099/jgv.0.000909. [Epub ahead of print]
[h=1]Human interactome of the influenza B virus NS1 protein.[/h] Patzina C[SUP]1[/SUP], Botting CH[SUP]2[/SUP], Garc?a-Sastre A[SUP]3[/SUP], Randall RE[SUP]2[/SUP], Hale BG[SUP]1[/SUP].
[h=3]Author information[/h]
[h=3]Abstract[/h] NS1 proteins of influenza A and B viruses share limited sequence homology, yet both are potent manipulators of host cell processes, particularly interferon (IFN) induction. Although many cellular partners are reported for A/NS1, only a few (e.g. PKR and ISG15) have been identified for B/NS1. Here, affinity-purification and mass spectrometry were used to expand the known host interactome of B/NS1. We identified 22 human proteins as new putative targets for B/NS1, validating several, including DHX9, ILF3, YBX1 and HNRNPC. Consistent with two RNA-binding domains in B/NS1, many of the identified factors bind RNA and some interact with B/NS1 in an RNA-dependent manner. Functional characterization of several B/NS1 interactors identified SNRNP200 as a potential positive regulator of host IFN responses, while ILF3 exhibited dual roles in both IFN induction and influenza B virus replication. These data provide a resource for future investigations into the mechanisms underpinning host cell modulation by influenza B virus NS1.
PMID: 28869005 DOI: 10.1099/jgv.0.000909
[h=1]Human interactome of the influenza B virus NS1 protein.[/h] Patzina C[SUP]1[/SUP], Botting CH[SUP]2[/SUP], Garc?a-Sastre A[SUP]3[/SUP], Randall RE[SUP]2[/SUP], Hale BG[SUP]1[/SUP].
[h=3]Author information[/h]
[h=3]Abstract[/h] NS1 proteins of influenza A and B viruses share limited sequence homology, yet both are potent manipulators of host cell processes, particularly interferon (IFN) induction. Although many cellular partners are reported for A/NS1, only a few (e.g. PKR and ISG15) have been identified for B/NS1. Here, affinity-purification and mass spectrometry were used to expand the known host interactome of B/NS1. We identified 22 human proteins as new putative targets for B/NS1, validating several, including DHX9, ILF3, YBX1 and HNRNPC. Consistent with two RNA-binding domains in B/NS1, many of the identified factors bind RNA and some interact with B/NS1 in an RNA-dependent manner. Functional characterization of several B/NS1 interactors identified SNRNP200 as a potential positive regulator of host IFN responses, while ILF3 exhibited dual roles in both IFN induction and influenza B virus replication. These data provide a resource for future investigations into the mechanisms underpinning host cell modulation by influenza B virus NS1.
PMID: 28869005 DOI: 10.1099/jgv.0.000909