Résumé
The
Escherichia coli maltose-binding protein is a highly versatile carrier protein allowing the construction of genetically engineered hybrid proteins. It accepts large fusions to both C- and N-termini as well as the insertion of shorter peptides at ‘permissive sites’ within the continuity of the protein. We have genetically inserted immunogenic peptides corresponding to defined viral B- and T-cell epitopes into two permissive sites: one at amino acid site 133, the other at site 303. The hybrid proteins are easily purifiable and immunogenic, inducing peptide-specific B- and T-cell responses. When delivered by live bacteria (
E. coli K12 and
aroA Salmonella typhimurium) antibody responses can be induced against both the
MalE carrier and the inserted B-cell epitope. We discuss the induction of T-cell responses by bacterial delivery systems.