Immunogenic and Protective Potentials of Recombinant Receptor Binding Domain and a C-Terminal Fragment of Clostridium botulinum Neurotoxin Type E
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Abstract:
Clostridium Botulinum Type E neurotoxin heavy chain consists of two domains: the translocation domain asthe N-terminal half and the binding domain as the Cterminal half (Hc). One effective way to neutralize botulinum neurotoxin is to inhibit binding of this toxin to neuromuscular synapses with antibodies against binding domain. Two synthetic genes, coding for Hc (the full length binding domain) and the c-terminal quarter of binding domain (HcQ), were cloned in pET-28a vector and over-expressed in E. coli BL21 (DE3) cells.These recombinant proteins were purified by affinity Ni-NTA column (under native condition). Mice werevaccinated with 2 μg of purified proteins, respectively; at step one with complete adjuvant, steps two andthree with incomplete adjuvant and step four only with phosphate buffered saline (PBS). Enzyme-linkedimmunosorbent assay (ELISA) has been performed with mice serum samples 14 days following their thirdand final vaccination. Binding activity of the purified proteins to ganglioside and synaptotagmin II was analyzed by ELISA. The results showed that HcQ and Hc could bind with ganglioside. Based on challengeexperiments it was revealed that HcQ, Hc and BoNT/E toxoid could give protections in mice challenged with102 , 104 and 105 minimum lethal dose (MLD) dose of BoNT/E.
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Recombinant proteins are tending to be the most favorable vaccine-candidates against botulism. Recombinant Carboxy-terminal of botulinum neurotoxin serotype E (rBoNT/E-HCC) has been introduced as an efficient vaccine against botulism type E. In this report, we made an effort to investigate the effect of different pH on protein structure to assess if rBoNT/E-HCC could be used as a vaccine for or...
full textthe effect of ph on recombinant c-terminal domain of botulinum neurotoxin type e (rbont/e-hcc)
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full textthe investigation of the relationship between type a and type b personalities and quality of translation
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Comparative Study of Immunological and Structural Properties of Two Recombinant Vaccine Candidates against Botulinum Neurotoxin Type E
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...
full textDNA vaccination using the fragment C of botulinum neurotoxin type A provided protective immunity in mice.
Botulinum neurotoxin (BoNT) is one of the most toxic substances known to produce severe neuromuscular paralysis. The currently used vaccine is prepared mainly from biohazardous toxins. Thus, we studied an alternative method and demonstrated that DNA immunization provided sufficient protection against botulism in a murine model. A plasmid of pBoNT/A-Hc, which encodes the fragment C gene of type ...
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Journal title
volume 9 issue 3
pages 181- 187
publication date 2011-07-01
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