Abstract
Influenza NS2 protein was expressed in Saccharomyces cerevisiae using a copper-inducible promoter. The protein produced had a molecular weight of 13 kDa, was reactive with anti-NS2 antiserum and was localised to the yeast cell nucleus. Two-hybrid analysis identified a direct protein-protein interaction between NS2 and the M2 protein of the virus, involving the C-terminal 163 residues of M1. A filter-binding assay localised the M1 binding region to the C-terminal 70 amino acids of NS2.
Publication types
-
Research Support, Non-U.S. Gov't
MeSH terms
-
Amino Acid Sequence
-
Base Sequence
-
Cloning, Molecular
-
DNA Primers / chemistry
-
Influenza A virus / genetics
-
Influenza A virus / metabolism*
-
Molecular Sequence Data
-
Protein Binding
-
Recombinant Proteins
-
Saccharomyces cerevisiae
-
Viral Matrix Proteins / metabolism*
-
Viral Nonstructural Proteins / genetics
-
Viral Nonstructural Proteins / metabolism*
Substances
-
DNA Primers
-
M-protein, influenza virus
-
M1 protein, Influenza A virus
-
M2 protein, Influenza A virus
-
Recombinant Proteins
-
Viral Matrix Proteins
-
Viral Nonstructural Proteins