biostudies-literatureKim YSGraduate School of YONSEI University Research Scholarship GrantsMinistry of Food and Drug Safety of the Republic of KoreaNational Research Foundation of Korea1990-2007https://www.ebi.ac.uk/biostudies/studies/S-EPMC7262357biostudies-literatureUnknown117(7)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 Biotechnology and bioengineeringBuilt-in RNA-mediated chaperone (chaperna) for antigen folding tailored to immunized hosts.PMC726235716172MFDS19916172MFDS36316172MFDS268NRF‐2018M3A9H4079358NRF-2018M3A9H407935818172MFDS252Cheong YSung JOh HLee EYNam JHSeong BLKim JChoi SCho NHLim JChae WKang SMKim YSfalseBuilt-in RNA-mediated chaperone (chaperna) for antigen folding tailored to immunized hosts.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 2020-01-01T00:00:00Z2020 Jul2026-05-07T06:34:33.027Z2020-06-05T07:06:53ZS-EPMC72623573229797210.1002/bit.27355