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Analysis of the PDZ binding specificities of Influenza A virus NS1 proteins.

Authors
  • Thomas, Miranda
  • Kranjec, Christian
  • Nagasaka, Kazunori
  • Matlashewski, Greg
  • Banks, Lawrence
Type
Published Article
Journal
Virology Journal
Publisher
Springer (Biomed Central Ltd.)
Publication Date
Jan 01, 2011
Volume
8
Pages
25–25
Identifiers
DOI: 10.1186/1743-422X-8-25
PMID: 21247458
Source
Medline
License
Unknown

Abstract

The Influenza A virus non-structural protein 1 (NS1) is a multifunctional virulence factor with several protein-protein interaction domains, involved in preventing apoptosis of the infected cell and in evading the interferon response. In addition, the majority of influenza A virus NS1 proteins have a class I PDZ-binding motif at the C-terminus, and this itself has been shown to be a virulence determinant.In the majority of human influenza NS1 proteins the consensus motif is RSxV: in avian NS1 it is ESxV. Of the few human strains that have the avian motif, all were from very high mortality outbreaks of the disease. Previous work has shown that minor differences in PDZ-binding motifs can have major effects on the spectrum of cellular proteins targeted. In this study we analyse the effect of these differences upon the binding of Influenza A virus NS1 protein to a range of cellular proteins involved in polarity and signal transduction.

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