Repository of Research and Investigative Information

Repository of Research and Investigative Information

Baqiyatallah University of Medical Sciences

Design and characterization of a chimeric multiepitope construct containing CfaB, heat-stable toxoid, CssA, CssB, and heat-labile toxin subunit B of enterotoxigenic Escherichia coli: a bioinformatic approach

(2014) Design and characterization of a chimeric multiepitope construct containing CfaB, heat-stable toxoid, CssA, CssB, and heat-labile toxin subunit B of enterotoxigenic Escherichia coli: a bioinformatic approach. Biotechnology and Applied Biochemistry. pp. 517-527. ISSN 0885-4513

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Abstract

Enterotoxigenic Escherichia coli (ETEC) strains are the most common cause of bacterial diarrhea in children in developing countries and travelers to these areas. Enterotoxins and colonization factors (CFs) are two key virulence factors in ETEC pathogenesis, and the heterogeneity of the CFs is the bottleneck in reaching an effective vaccine. In this study, a candidate subunit vaccine, which is composed of CfaB, CssA and CssB, structural subunits of colonization factor antigen I and CS6 CFs, labile toxin subunit B, and the binding subunit of heat-labile and heat-stable toxoid, was designed to provide broad-spectrum protection against ETEC. The different features of chimeric gene, its mRNA stability, and chimeric protein properties were analyzed by using bioinformatic tools. The optimized chimeric gene was chemically synthesized and expressed successfully in a prokaryotic host. The purified protein was used for assessment of bioinformatic data by experimental methods. (C) 2013 International Union of Biochemistry and Molecular Biology, Inc.

Item Type: Article
Keywords: enterotoxigenic Escherichia coli bioinformatics analysis chimeric protein immunogenicity protein secondary structure colonization-factor structure prediction virulence factors cell epitopes vaccine server cs6 purification expression Biochemistry & Molecular Biology Biotechnology & Applied Microbiology
Divisions:
Page Range: pp. 517-527
Journal or Publication Title: Biotechnology and Applied Biochemistry
Journal Index: ISI
Volume: 61
Number: 5
Identification Number: https://doi.org/10.1002/bab.1196
ISSN: 0885-4513
Depositing User: مهندس مهدی شریفی
URI: http://eprints.bmsu.ac.ir/id/eprint/5740

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