Volume 16, Issue 4 (10-2012)                   ibj 2012, 16(4): 185-192 | Back to browse issues page


XML Print


Download citation:
BibTeX | RIS | EndNote | Medlars | ProCite | Reference Manager | RefWorks
Send citation to:

Rostamian M, Mousavy S J, Ebrahimi F, Ghadami S A, Sheibani N, Minaei M E et al . Comparative Study of Immunological and Structural Properties of Two Recombinant Vaccine Candidates against Botulinum Neurotoxin Type E. ibj. 2012; 16 (4) :185-192
URL: http://ibj.pasteur.ac.ir/article-1-773-en.html
Abstract:  
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.
Type of Study: Full Length | Subject: Related Fields

Add your comments about this article : Your username or Email:
CAPTCHA

Send email to the article author


© 2020 All Rights Reserved | Iranian Biomedical Journal

Designed & Developed by : Yektaweb