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Identification of Influenza C Virus Phosphoproteins
Author(s) -
Nishimura Hidekazu,
Sugawara Kanetsu,
Gao Peng,
Muraki Yasushi,
Hongo Seiji,
Kitame Fumio,
Nakamura Kiyoto
Publication year - 1995
Publication title -
microbiology and immunology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.664
H-Index - 70
eISSN - 1348-0421
pISSN - 0385-5600
DOI - 10.1111/j.1348-0421.1995.tb03251.x
Subject(s) - biology , phosphorylation , viral matrix protein , glycoprotein , trypsin , virus , nucleoprotein , hemagglutinin (influenza) , monoclonal antibody , orthomyxoviridae , proteolysis , microbiology and biotechnology , virology , biochemistry , enzyme , influenza a virus , antibody , immunology
The HMV‐II cells infected with influenza C virus were labeled with inorganic [ 32 P]phosphate to identify phosphorylated proteins. Analysis by radioimmunoprecipitation with antiviral serum or monoclonal antibodies revealed that three major structural proteins of the virus, hemagglutinin‐esterase (HE), nucleoprotein (NP), and matrix protein (M1) are all phosphorylated in both infected cells and virions. It was also observed that, in the presence of trypsin (10 μg/ml), the unphosphorylated form of the HE glycoprotein was cleaved efficiently whereas the phosphorylated form was not, raising the possibility that phosphorylation of HE may influence its susceptibility to degradation by proteolytic enzymes.