Chimeric Fimbrial Multiepitope Antigen Fused to Double-Mutant LT (dmLT) Induces Antibodies That Inhibit Enterotoxigenic <i>E. coli</i> Adhesion in Porcine IPEC-J2 Cells.

ABSTRACT: This study focused on utilizing the double-mutant heat-labile toxin (R192G/L211A) (dmLT) as a backbone protein, into which neutralizing epitopes of ETEC (FaeG, FedF, FanC, FasA, and Fim41a) were embedded. A combination of computational modeling and immunogenicity analysis was conducted to evaluate the dmLT_{(R192G/L211A)} multiepitope fusion antigen (MEFA). Both the computational modeling and experimental results confirmed that all relevant epitopes were clearly exposed on the surface of the MEFA. Subcutaneous immunizations of rabbits with the MEFA protein yielded the development of IgG antibodies that targeted all five fimbriae. Furthermore, these antibodies demonstrated significant inhibition of adhesion for K88+, K99+, 987P+, F18+, and F41+ ETEC strains to porcine small intestin

SUBMITTER: He J 

PROVIDER: S-EPMC12523420 | biostudies-literature | 2025 Sep

REPOSITORIES: biostudies-literature