{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Jiang L"],"funding":["National Natural Science Foundation of China"],"pagination":["e0117522"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC9555151"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["96(19)"],"pubmed_abstract":["The frequent outbreak of grass carp hemorrhagic disease caused by grass carp reovirus (GCRV), especially the mainly prevalent type II GCRV (GCRV-II), has seriously affected the grass carp culture in China. However, its pathogenic mechanism is still far from clear. In this study, the GCRV-II outer capsid protein VP35 was used as bait to capture interacting partners from <i>Ctenopharyngon idellus</i> kidney (CIK) cells, and heat shock protein 90 (Hsp90) was selected and confirmed interacting with VP35 through the C-terminal domain of Hsp90. Knockdown of Hsp90 or inhibition of Hsp90 activity suppressed GCRV-II proliferation, demonstrating that Hsp90 is an essential factor for GCRV-II proliferation. The confocal microscopy and flow cytometry showed that Hsp90 localized at both membrane and cyt"],"journal":["Journal of virology"],"pubmed_title":["Hsp90 Regulates GCRV-II Proliferation by Interacting with VP35 as Its Receptor and Chaperone."],"pmcid":["PMC9555151"],"funding_grant_id":["31972832","31725026","32173014","31930114"],"pubmed_authors":["Jiang L","Liu AQ","Zhang YA","Zhang C","Tu J"],"additional_accession":[]},"is_claimable":false,"name":"Hsp90 Regulates GCRV-II Proliferation by Interacting with VP35 as Its Receptor and Chaperone.","description":"The frequent outbreak of grass carp hemorrhagic disease caused by grass carp reovirus (GCRV), especially the mainly prevalent type II GCRV (GCRV-II), has seriously affected the grass carp culture in China. However, its pathogenic mechanism is still far from clear. In this study, the GCRV-II outer capsid protein VP35 was used as bait to capture interacting partners from <i>Ctenopharyngon idellus</i> kidney (CIK) cells, and heat shock protein 90 (Hsp90) was selected and confirmed interacting with VP35 through the C-terminal domain of Hsp90. Knockdown of Hsp90 or inhibition of Hsp90 activity suppressed GCRV-II proliferation, demonstrating that Hsp90 is an essential factor for GCRV-II proliferation. The confocal microscopy and flow cytometry showed that Hsp90 localized at both membrane and cyt","dates":{"release":"2022-01-01T00:00:00Z","publication":"2022 Oct","modification":"2026-06-14T07:50:41.548Z","creation":"2025-02-18T23:35:20.93Z"},"accession":"S-EPMC9555151","cross_references":{"pubmed":["36102647"],"doi":["10.1128/jvi.01175-22"]}}