%0 Journal Article %A Rostamian, Mosayeb %A Mousavy, Seyed Jafar %A Ebrahimi, Firouz %A Ghadami, Seyyed Abolghasem %A Sheibani, Nader %A Minaei, Mohammad Ebrahim %A Arefpour Torabi, Mohammad Ali %T Comparative Study of Immunological and Structural Properties of Two Recombinant Vaccine Candidates against Botulinum Neurotoxin Type E %J Iranian Biomedical Journal %V 16 %N 4 %U http://ibj.pasteur.ac.ir/article-1-773-en.html %R 10.6091/ibj.1076.2012 %D 2012 %K Botulinum neurotoxin type E (BoNT/E), Cross ELISA, circular dichroism, Computational modeling, recombinant vaccine-candidates, %X 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. %> http://ibj.pasteur.ac.ir/article-1-773-en.pdf %P 185-192 %& 185 %! Comparison of Two Recombinant Vaccine Candidates for Botulism %9 Full Length/Original Article %L A-10-1-372 %+ %G eng %@ 1028-852X %[ 2012