Comparative Study of Immunological and Structural Properties of Two Recombinant Vaccine Candidates against Botulinum Neurotoxin Type E |
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| Authors: | Mosayeb Rostamian Seyed Jafar Mousavy Firouz Ebrahimi Seyyed Abolghasem Ghadami Nader Sheibani Mohammad Ebrahim Minaei Mohammad Ali Arefpour Torabi |
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| Institution: | 1.Dept. of Biology, Faculty of Basic Sciences, Imam Hussein University, Tehran, Iran;;2.Dept. of Biology, Faculty of Sciences, Razi University, Kermanshah, Iran;;3.Medical Biology Research Center, Kermanshah University of Medical Science, Kermanshah, Iran;;4.Dept. of Ophthalmology and Visual Sciences and Pharmacology, University of Wisconsin School of Medicine and Public Health, Madison, WI, USA |
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| Abstract: | BackgroundRecently, 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).MethodsThe 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. ConclusionThe 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. Iran. Biomed. Key Words: Botulinum neurotoxin type E (BoNT/E), Cross ELISA, circular dichroism, Computational modeling, recombinant vaccine-candidates |
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