In silico study of FlaA protein from various Campylobacter species revealing B-cell and T-cell epitope similarities

Campylobacter sp. is a gram-negative bacterium that is commonly contaminated in poultry or processed poultry industry. The consuming of Campylobacter sp. contaminated food is a major cause of Campylobacteriosis which most patient becomes diarrhea, abdominal pain, nausea and mild to severe fever for a week. The common Campylobacter sp. that generally infects in humans are C. jejuni, C. coli, C. lari. Currently, it is found that many species of Campylobacter are considered to be a drug-resistance microorganism which many classes of antibiotics are difficult to control on dosmestic or even in industrial scale. However, one of the excellent strategies for prevent Campylobacter infection is to stimulate the host's immune system through vaccination. Therefore, in this research, we are interested in evaluating FlaA protein which is the major component of Campylobacter’s flagellar with the reason that; 1) FlaA is the most abundant and high antigenicity protein, 2) it is produced throughout the life of bacteria, and 3) FlaA is located on cell surface which is easily to recognized by antibody. The results of the experiment including the comparison of amino acid sequence alignment, three-dimensional structure analysis, and the B cell and T cell epitope prediction of the Campylobacter FlaA 3 species, revealed that there are many conserved epitopes located on FlaA 3D structure species which might be able to recognized by the similar series of host immune system. These results suggest that the use of FlaA in C. jejuni may be of interest in vaccine development to be applied for prevention of broad-spectrum Campylobacter infection.