Abstract

BackgroundCampylobacter jejuni is a potent bacterial pathogen culpable for diarrheal disease called campylobacteriosis. It is realized as a major health issue attributable to unavailability of appropriate vaccines and clinical treatment options. As other pathogens, C. jejuni entails host cellular components of an infected individual to disseminate this disease. These host–pathogen interfaces during C. jejuni infection are complex, vibrant and involved in the nicking of host cell environment, enzymes and pathways. Existing therapies are trusted only on a much smaller number of drugs, most of them are insufficient because of their severe host toxicity or drug-resistance phenomena. To find out remedial alternatives, the identification of new biotargets is highly anticipated. Understanding the molecules involved in pathogenesis has the potential to yield new and exciting strategies for therapeutic intervention. In this direction, advances in bioinformatics have opened up new possibilities for the rapid measurement of global changes during infection and this could be exploited to understand the molecular interactions involved in campylobacteriosis.MethodsIn this study, homology modeling, epitope prediction and identification of ligand binding sites has been explored. Further attempt to generate strapping 3D model of cytolethal distending toxin protein from C. jejuni have been described for the first time.ResultsCDT protein isolated from C. jejuni was analyzed using various bioinformatics and immuno-informatics tools including sequence and structure tools. A total of fifty five antigenic determinants were predicted and prediction results of CTL epitopes revealed that five MHC ligand are found in CDT. The three potential pocket binding site are found in the sequence that can be useful for drug designing.ConclusionsThis model, we hope, will be of help in designing and predicting novel CDT inhibitors and vaccine candidates.

Highlights

  • Campylobacter jejuni is a potent bacterial pathogen culpable for diarrheal disease called campylobacteriosis

  • The current study was originated to perform structure based sequence analysis of the Cytolethal distending toxins (CDT) protein isolated from C. jejuni

  • The protein sequence was obtained from the NCBI protein database using accession number gi| 205345645|gb|EDZ32284.1| cytolethal distending toxin [Campylobacter jejuni]

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Summary

Introduction

Campylobacter jejuni is a potent bacterial pathogen culpable for diarrheal disease called campylobacteriosis. Campylobacter is extensively distributed in poultry; cattle, pigs, sheep, and pet animals may be a source of these microorganisms This infection may be due to either eating of semi cooked meat or crosscontamination of ready-to-eat food at the time of Cytolethal distending toxins (CDT) are a class of heterotrimeric toxins produced by C. jejuni and by closely related spp., such as C. fetus, C. coli [4,5], Shigella [6] and Escherichia coli [7]. The CDT comprises of three protein subunits namely CdtA, CdtB, and CdtC causes progressive cellular distention with ultimate cell death and have been proposed as virulence factors in the pathogenesis of C. jejuni [9] These results suggest that the CDTs are involved invasion, survival and internalization into the host cell [10,11,12,13]. CDT from C. jejuni has been studied and characterized in laboratory [14,15], but research on immune responses and pathogenesis of C. jejuni remains unexploited

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