Characterization of structural and immunological properties of a fusion protein between flagellin from Salmonella and lumazine synthase from Brucella.

HIRIART YANINA,; ROSSI ANDRE; BIEDMA MARINA; ERREA AGUSTINA; GRISELDA MORENO; DELPHINE CAYET; RINALDI JIMENA; BLANCA BRUNO; JEAN CLAUDE SIRARD; FERNANDO GOLDBAUM; BERGUER PAULA; MARTIN RUMBO

PROTEIN SCIENCE

JOHN WILEY & SONS INC

Lugar: New York; Año: 2017

0961-8368

Aiming to combine the flexibility of Brucella Lumazine synthetase (BLS) to adapt different protein domains in a decameric structure and the capacity of BLS and flagellin to enhance the immunogenicity of peptides that are linked to their structure, we generated a chimeric protein (BLS-FliC131) by fusing flagellin from Salmonella in the N-termini of BLS. The obtained protein was recognized by anti-flagellin and anti-BLS antibodies, keeping the oligomerization capacity of BLS, without affecting the folding of the monomeric protein components determined by circular dichroism. Furthermore, the thermal stability of each fusion partner is conserved, indicating that the interactions that participate in its folding are not affected by the genetic fusion. Besides, either in vitro or in vivo using TLR5 deficient animals we could determine that BLS-FliC131 retains the capacity of triggering TLR5. The humoral response against BLS elicited by BLS-FliC131 was stronger than the one elicited by equimolar amounts of BLS + FliC. Since BLS scaffold allows the generation of hetero-decameric structures, we expect that flagellin oligomerization on this protein scaffold will generate a new vaccine platform with enhanced capacity to activate immune responses.