Influenza B virus non-structural protein 1 counteracts ISG15 antiviral activity by sequestering ISGylated viral proteins

Chen Zhao; Haripriya Sridharan; Ran Chen; Darren P. Baker; Shanshan Wang; Robert M. Krug

doi:10.1038/ncomms12754

Nature Communications (Sep 2016)

Influenza B virus non-structural protein 1 counteracts ISG15 antiviral activity by sequestering ISGylated viral proteins

Chen Zhao,
Haripriya Sridharan,
Ran Chen,
Darren P. Baker,
Shanshan Wang,
Robert M. Krug

Affiliations

Chen Zhao: Department of Molecular Biosciences, Center for Infectious Disease, Institute for Cellular and Molecular Biology, University of Texas at Austin
Haripriya Sridharan: Department of Molecular Biosciences, Center for Infectious Disease, Institute for Cellular and Molecular Biology, University of Texas at Austin
Ran Chen: Department of Molecular Biosciences, Center for Infectious Disease, Institute for Cellular and Molecular Biology, University of Texas at Austin
Darren P. Baker: Biogen, Inc.
Shanshan Wang: Department of Molecular Biosciences, Center for Infectious Disease, Institute for Cellular and Molecular Biology, University of Texas at Austin
Robert M. Krug: Department of Molecular Biosciences, Center for Infectious Disease, Institute for Cellular and Molecular Biology, University of Texas at Austin

DOI: https://doi.org/10.1038/ncomms12754
Journal volume & issue: Vol. 7, no. 1
pp. 1 – 12

Abstract

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The ubiquitin-like protein ISG15 can be covalently linked to cellular and viral proteins, but the consequences of this ‘ISGylation’ remain largely unknown. Here, Zhao et al.show that ISGylation of the influenza B virus nucleoprotein inhibits formation of a functional viral replication complex.

Published in Nature Communications

ISSN: 2041-1723 (Online)
Publisher: Nature Portfolio
Country of publisher: United Kingdom
LCC subjects: Science
Website: https://www.nature.com/ncomms/

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