comparative study of immunological and structural properties of two recombinant vaccine candidates against botulinum neurotoxin type e
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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.
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Journal title:
iranian biomedical journalجلد ۱۶، شماره ۴، صفحات ۱۸۵-۱۹۲
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