A recombinant subunit vaccine based on the insertion of 27 amino acids from Omp31 to the N-terminus of BLS induced a similar degree of protection againstB. ovisthanRev.1vaccination

• Published in: Vaccine Vol. 25; no. 22; p. 4437
• Main Authors: Cassataro, Juliana, Pasquevich, Karina A, Estein, Silvia M, Laplagne, Diego A, Velikovsky, Carlos A, de la Barrera, Silvia, Bowden, Raúl, Fossati, Carlos A, Giambartolomei, Guillermo H, Goldbaum, Fernando A
• Format: Journal Article
• Language: English
• Published: Kidlington Elsevier Limited 30.05.2007
• Subjects: Amino acids; Bacteriology; Brucellosis; Infections; Peptides; Proteins; Vaccines
• ISSN: 0264-410X; 1873-2518
• DOI: 10.1016/j.vaccine.2007.03.028

The development of an effective subunit vaccine against brucellosis is a research area of intense interest. The enzyme lumazine synthase fromBrucellaspp. (BLS) is highly immunogenic, presumably due to its decameric arrangement and remarkable stability. In this work we decided to develop a chimera with the scaffold protein BLS decorated with 10 copies of a known protective epitope derived from an outer membrane protein of 31kDa (Omp31) fromBrucellaspp. Vaccination of BALB/c mice with the chimera as a recombinant protein (rBLSOmp31) provided the best protection level againstBrucella ovis, which was higher than the given by the co-delivery of both recombinant proteins (rBLS+rOmp31) and similar than the control vaccineBrucella melitensisstrainRev.1. Moreover rBLSOmp31 induced protection againstBrucella melitensisbut to a lesser degree thanRev.1. The chimera induced a strong humoral response against the inserted peptide. It also induced peptide- and BLS-specific T helper 1 and cytotoxic T responses. In conclusion, our results indicate that BLSOmp31 could be a useful candidate for the development of subunit vaccines against brucellosis since it elicits humoral, T helper and cytotoxic immune responses and protection against smooth and rough species ofBrucella.