{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Kim YS"],"funding":["Graduate School of YONSEI University Research Scholarship Grants","Ministry of Food and Drug Safety of the Republic of Korea","National Research Foundation of Korea"],"pagination":["1990-2007"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC7262357"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["117(7)"],"pubmed_abstract":["High-quality antibody (Ab) production depends on the availability of immunologically relevant antigens. We present a potentially universal platform for generating soluble antigens from bacterial hosts, tailored to immunized animals for Ab production. A novel RNA-dependent chaperone, in which the target antigen is genetically fused with an RNA-interacting domain (RID) docking tag derived from the immunized host, promotes the solubility and robust folding of the target antigen. We selected the N-terminal tRNA-binding domain of lysyl-tRNA synthetase (LysRS) as the RID for fusion with viral proteins and demonstrated the expression of the RID fusion proteins in their soluble and native conformations; immunization predominantly elicited Ab responses to the target antigen, whereas the \"self\" RID "],"journal":["Biotechnology and bioengineering"],"pubmed_title":["Built-in RNA-mediated chaperone (chaperna) for antigen folding tailored to immunized hosts."],"pmcid":["PMC7262357"],"funding_grant_id":["16172MFDS199","16172MFDS363","16172MFDS268","NRF‐2018M3A9H4079358","NRF-2018M3A9H4079358","18172MFDS252"],"pubmed_authors":["Cheong Y","Sung J","Oh H","Lee EY","Nam JH","Seong BL","Kim J","Choi S","Cho NH","Lim J","Chae W","Kang SM","Kim YS"],"additional_accession":[]},"is_claimable":false,"name":"Built-in RNA-mediated chaperone (chaperna) for antigen folding tailored to immunized hosts.","description":"High-quality antibody (Ab) production depends on the availability of immunologically relevant antigens. We present a potentially universal platform for generating soluble antigens from bacterial hosts, tailored to immunized animals for Ab production. A novel RNA-dependent chaperone, in which the target antigen is genetically fused with an RNA-interacting domain (RID) docking tag derived from the immunized host, promotes the solubility and robust folding of the target antigen. We selected the N-terminal tRNA-binding domain of lysyl-tRNA synthetase (LysRS) as the RID for fusion with viral proteins and demonstrated the expression of the RID fusion proteins in their soluble and native conformations; immunization predominantly elicited Ab responses to the target antigen, whereas the \"self\" RID ","dates":{"release":"2020-01-01T00:00:00Z","publication":"2020 Jul","modification":"2026-05-07T06:34:33.027Z","creation":"2020-06-05T07:06:53Z"},"accession":"S-EPMC7262357","cross_references":{"pubmed":["32297972"],"doi":["10.1002/bit.27355"]}}