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Identification of annexin 33 kDa in cultured cells as a binding protein of influenza viruses
Author(s) -
Otto Matthias,
Günther Anna,
Fan Hua,
Rick Oliver,
Huang Richard T.C.
Publication year - 1994
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(94)01241-5
Subject(s) - sialic acid , binding protein , glycoprotein , annexin , annexin a2 , microbiology and biotechnology , orthomyxoviridae , virus , biology , calcium binding protein , biochemistry , molecular mass , influenza a virus , chemistry , cell , virology , calcium , gene , enzyme , organic chemistry
The binding of three influenza A and one influenza B virus strains to proteins of three continuously cultured cell lines was studied using protein overlay and immunostaining methods. The results obtained indicated the presence of both sialic acid‐dependent and ‐independent binding of the virus strains; virus binding to proteins in the molecular mass range from about 40 to 103 kDa was dependent on sialic acid, whereas binding to the 33 kDa protein was independent of sialic acid. The 33 kDa binding protein was identified as annexin, a widely distributed non‐glycosylated calcium‐dependent phospholipid‐binding protein.