Human interactome of the influenza B virus NS1 protein

Corinna Patzina; Catherine H. Botting; Adolfo García-Sastre; Richard E. Randall; Benjamin G. Hale

doi:10.1099/jgv.0.000909

Human interactome of the influenza B virus NS1 protein

Corinna Patzina, Catherine H. Botting, Adolfo García-Sastre, Richard E. Randall, Benjamin G. Hale^*

^*Corresponding author for this work

Research output: Contribution to journal › Article › peer-review

Abstract

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.

Original language	English
Article number	000909
Pages (from-to)	2267-2273
Number of pages	7
Journal	Journal of General Virology
Volume	98
Issue number	9
DOIs	https://doi.org/10.1099/jgv.0.000909
Publication status	Published - 1 Sept 2017

Keywords

Influenza
Interferon
Proteomics
Virulence factor
Virus-host interaction

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10.1099/jgv.0.000909Licence: CC BY

Botting_2017_JGV_HumanInteractome_CC
© 2017 The Authors. This is an open access article under the terms of the http://creativecommons.org/licenses/by/4.0/, which permits unrestricted use, distribution and reproduction in any medium, provided the original author and source are credited.
Final published version, 2.04 MBLicence: CC BY

MaXis ESI QTOF mass spectrometer: Equipment only grant-Mass spectrometers for Proteomics, Lipidomics and focused Metabolomics research
Botting, C. H. (PI), Elliott, R. M. (CoI), Randall, R. E. (CoI), Smith, T. K. (CoI) & White, M. (CoI)
The Wellcome Trust
1/08/11 → 31/07/14
Project: Standard

Cite this

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title = "Human interactome of the influenza B virus NS1 protein",

abstract = "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.",

keywords = "Influenza, Interferon, Proteomics, Virulence factor, Virus-host interaction",

author = "Corinna Patzina and Botting, {Catherine H.} and Adolfo Garc{\'i}a-Sastre and Randall, {Richard E.} and Hale, {Benjamin G.}",

note = "This work was partially supported by NIAID grant U19AI106754, and by CRIP (Center for Research in Influenza Pathogenesis), an NIAID funded Center of Excellence for Influenza Research and Surveillance (CEIRS, contract #HHSN272201400008C) to A. G-S. Work at the University of Zurich was supported by the Swiss National Science Foundation (grant 31003A_159993 to BGH).",

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AU - Hale, Benjamin G.

N1 - This work was partially supported by NIAID grant U19AI106754, and by CRIP (Center for Research in Influenza Pathogenesis), an NIAID funded Center of Excellence for Influenza Research and Surveillance (CEIRS, contract #HHSN272201400008C) to A. G-S. Work at the University of Zurich was supported by the Swiss National Science Foundation (grant 31003A_159993 to BGH).

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N2 - 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.

AB - 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.

KW - Influenza

KW - Interferon

KW - Proteomics

KW - Virulence factor

KW - Virus-host interaction

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Human interactome of the influenza B virus NS1 protein

Abstract

Keywords

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MaXis ESI QTOF mass spectrometer: Equipment only grant-Mass spectrometers for Proteomics, Lipidomics and focused Metabolomics research

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