Built-in RNA-mediated chaperone (chaperna) for antigen folding tailored to immunized hosts.

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

SUBMITTER: Kim YS 

PROVIDER: S-EPMC7262357 | biostudies-literature | 2020 Jul

REPOSITORIES: biostudies-literature