Comparative study of immunological and structural properties of two recombinant vaccine candidates against botulinum neurotoxin type E.

Publications // Sheibani Lab // Jan 01 2012

PubMed ID: 23183617

Author(s): Rostamian M, Mousavy SJ, Ebrahimi F, Ghadami SA, Sheibani N, Minaei ME, Arefpour Torabi MA. Comparative study of immunological and structural properties of two recombinant vaccine candidates against botulinum neurotoxin type E. Iran Biomed J. 2012;16(4):185-92. PMID 23183617

Journal: Iranian Biomedical Journal, Volume 16, Issue 4, 2012

BACKGROUND Recently, botulinum neurotoxin (BoNT)-derived recombinant proteins have been suggested as potential botulism vaccines. Here, with concentrating on BoNT type E (BoNT/E), we studied two of these binding domain-based recombinant proteins: a multivalent chimer protein, which is composed of BoNT serotypes A, B and E binding subdomains, and a monovalent recombinant protein, which contains 93 amino acid residues from recombinant C-terminal heavy chain of BoNT/E (rBoNT/E-HCC). Both proteins have an identical region (48 aa) that contains one of the most important BoNT/E epitopes (YLTHMRD sequence).

METHODS The recombinant protein efficiency in antibody production, their structural differences, and their BoNT/E-epitope location were compared by using ELISA, circular dichroism, computational modeling, and hydrophobicity predictions.

RESULTS Immunological studies indicated that the antibody yield against rBoNT/E-HCC was higher than chimer protein. Cross ELISA confirmed that the antibodies against the chimer protein recognized rBoNT/E-HCC more efficiently. However, both antibody groups (anti-chimer and anti-rBoNT/E-HCC antibodies) were able to recognize other proteins. Structural studies with circular dichroism showed that chimer proteins have slightly more secondary structures than rBoNT/E-HCC.

CONCLUSION The immunological results suggested that the above-mentioned identical region in rBoNT/E-HCC is more exposed. Circular dichroism, computational protein modeling and hydrophobicity predictions indicated a more exposed location for the identical region in rBoNT/E-HCC than the chimer protein, which is strongly in agreement with immunological results.