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Influenza A virus neuraminidase protein interacts with Hsp90, to stabilize itself and enhance cell survival
Author(s) -
Kumar Purnima,
Gaur Pratibha,
Kumari Rashmi,
Lal Sunil K
Publication year - 2019
Publication title -
journal of cellular biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.028
H-Index - 165
eISSN - 1097-4644
pISSN - 0730-2312
DOI - 10.1002/jcb.27935
Subject(s) - hsp90 , microbiology and biotechnology , neuraminidase , heat shock protein , immunoprecipitation , chaperone (clinical) , biology , virus , transfection , influenza a virus , cytoplasm , virology , biochemistry , gene , medicine , pathology
Neuraminidase protein (NA) of influenza A virus (IAV) is popularly known for its sialidase function to assist in the release of progeny virus. However, involvement of NA in other stages of the IAV life cycle also indicates its multifunctional nature and necessity to interact with other host proteins. Here, we report a host protein—heat shock protein 90 (Hsp90), as a novel interacting partner of IAV NA. A classical yeast two‐hybrid screen was conducted to identify a new host interacting partner for NA and the interaction was further validated by coimmunoprecipitation from cells, transiently expressing both proteins and also from IAV‐infected cells. Confocal imaging showed that both proteins colocalized in the cytoplasm in transfected host cells. Interestingly, increased levels of NA in the presence of Hsp90 was observed, which tends to decrease if adenosine triphosphatase activity of Hsp90 is inhibited using 17‐ N ‐allylamino‐17‐demethoxygeldanamycin (17AAG). This establishes viral NA as a client protein of host chaperone Hsp90 contributing toward NA's stability via the NA‐Hsp90 interaction. This is the first report showing the interaction of NA with Hsp90 and its role in stabilizing viral NA thus preventing it from degradation. Enhanced cell survival in the presence of this interaction was also observed, thus suggesting the requirement of stable viral NA, post‐IAV infection, for efficient virus production in infected mammalian cells.