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Paper Information

Journal:   IRANIAN JOURNAL OF PUBLIC HEALTH   AUGUST 2014 , Volume 43 , Number SUPPLEMENT 2; Page(s) 65 To 65.
 
Paper: 

ADHESION SITE OF BOTULINAL TOXIN: IS IT A PROPER VACCINE CANDIDATE?

 
 
Author(s):  POORMONTASERI MARYAM*, HOSEINZADEH SAEED, SADEGHI SARVESTANI MOHAMMAD VAHID
 
* FOOD HYGIENE, VETERINARY SCHOOL, SHIRAZ UNIVERSITY, SHIRAZ, IRAN
 
Abstract: 

Background: The botulinum neurotoxins are the causative agents of botulism and represent a family of seven structurally similar but antigenically distinct serotypes (A to G). The toxins exert their action by blocking the release of the neurotransmitter acetylcholine at the neuromuscular junction. The toxin consists of a 100 kDa heavy chain and 50 kDa light chain held together by a single disulfide bond. The carboxyterminal (Hc) fragment of botulinum toxin B (BHc) in E. coli strain GM2163 was expressed and evaluated in this study.
Methods: All strains of E. coli used in this study were primarily cultured on LB broth. The appropriate media were supplemented with ampicillin. DNA fragments which had been generated using the PCR and the synthetic gene was digested cloned into Hind III and Nco I digested plasmid PTG19-T and transformed into E. coli strain GM2163. The nucleotide sequence of the cloned fragment was determined to ensure authenticity.
Results: Based on deduced amino acid sequence homology with the Hc fragment of botulinum toxin a DNA fragment (1280 bp) was identified which would encode 428 amino acids at the C-terminus of heavy chain of botulinum toxin B. To enhance gene expression in E. coli a gene encoding the BHc was designed to reduce. The complete bhc gene, was created by ligating of the blocks to each other and cloning into plasmid vector in E. coli.
Conclusion: It could be suggested to produce a subunit vaccine based on the Hc binding domain of C. botulinum toxin type B which can protect against intra-peritoneal toxin challenge.

 
Keyword(s): CLOSTRIDIUM BOTULINUM, BHC GENE, VACCINE
 
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