{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Yang SW"],"funding":["Ministry of Agriculture, Food and Rural Affairs"],"pagination":["2658-2675"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC5901386"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["32(5)"],"pubmed_abstract":["A novel protein-folding function of RNA has been recognized, which can outperform previously known molecular chaperone proteins. The RNA as a molecular chaperone (chaperna) activity is intrinsic to some ribozymes and is operational during viral infections. Our purpose was to test whether influenza hemagglutinin (HA) can be assembled in a soluble, trimeric, and immunologically activating conformation by means of an RNA molecular chaperone (chaperna) activity. An RNA-interacting domain (RID) from the host being immunized was selected as a docking tag for RNA binding, which served as a transducer for the chaperna function for de novo folding and trimeric assembly of RID-HA1. Mutations that affect tRNA binding greatly increased the soluble aggregation defective in trimer assembly, suggesting t"],"journal":["FASEB journal : official publication of the Federation of American Societies for Experimental Biology"],"pubmed_title":["Harnessing an RNA-mediated chaperone for the assembly of influenza hemagglutinin in an immunologically relevant conformation."],"pmcid":["PMC5901386"],"funding_grant_id":["716002‐7"],"pubmed_authors":["Choi SI","Kwon SB","Byun YH","Seong BL","Lee YJ","Chae W","Kim CK","Yang SW","Kim P","Park C","Kim YS","Jang YH"],"additional_accession":[]},"is_claimable":false,"name":"Harnessing an RNA-mediated chaperone for the assembly of influenza hemagglutinin in an immunologically relevant conformation.","description":"A novel protein-folding function of RNA has been recognized, which can outperform previously known molecular chaperone proteins. The RNA as a molecular chaperone (chaperna) activity is intrinsic to some ribozymes and is operational during viral infections. Our purpose was to test whether influenza hemagglutinin (HA) can be assembled in a soluble, trimeric, and immunologically activating conformation by means of an RNA molecular chaperone (chaperna) activity. An RNA-interacting domain (RID) from the host being immunized was selected as a docking tag for RNA binding, which served as a transducer for the chaperna function for de novo folding and trimeric assembly of RID-HA1. Mutations that affect tRNA binding greatly increased the soluble aggregation defective in trimer assembly, suggesting t","dates":{"release":"2018-01-01T00:00:00Z","publication":"2018 May","modification":"2026-04-30T18:54:50.729Z","creation":"2019-03-26T23:45:40Z"},"accession":"S-EPMC5901386","cross_references":{"pubmed":["29295864"],"doi":["10.1096/fj.201700747RR"]}}