Critical role of neighbouring sequences on the immunogenicity of the C3 poliovirus neutralization epitope expressed at the surface of recombinant bacteria.

Abstract The C3 neutralization epitope of poliovirus type 1 (PV-1) is a continuous epitope comprised within residues 93–103 of capsid protein VP1. These residues form a loop at the surface of the virus particle. The authors compared the immunogenicity of two peptides which contain this epitope, when presented at the surface of Escherichia coli by genetic insertion in the outer membrane protein LamB. One peptide was 13 residues long (VP1:93–103) and the other one contained flanking sequences increasing its size to 35 residues (VP1:86–115). Mice and rabbits were immunized with recombinant bacteria expressing the corresponding LamB-VP1 hybrid proteins. Antibodies against synthetic peptides, against native and heat denatured viral particles, as well as neutralizing antibodies were monitored. In this mode of presentation the shortest form of the epitope was more immunogenic. We provide evidence that the conformation of the epitope is different in the two hybrid LamB proteins and discuss possible consequences for immunogenicity.