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Campylobacter jejuni  and  Campylobacter coli  are the most common cause of bacterial gastroenteritis worldwide. Additionally,  C .  jejuni  is the most common bacterial etiological agent in the autoimmune Guillain-Barré syndrome (GBS). Ganglioside mimicry by  C .  jejuni  lipooligosaccharide (LOS) is the triggering factor of the disease. LOS-associated genes involved in the synthesis and transfer of sialic acid (glycosyltranferases belonging to family GT-42) are essential in  C .  jejuni  to synthesize ganglioside-like LOS. Despite being isolated from GBS patients, scarce genetic evidence supports  C .  coli  role in the disease. In this study, through data mining and bioinformatics analysis,  C .  coli  is shown to possess a larger GT-42 glycosyltransferase repertoire than  C .  jejuni . Although GT-42 glycosyltransferases are widely distributed in  C .  coli  population, only a fraction of  C .  coli  strains (1%) are very likely able to express ganglioside mimics. Even though the activity of  C .  coli  specific GT-42 enzymes and their role in shaping the bacterial population are yet to be explored, evidence presented herein suggest that loss of function of some LOS-associated genes occurred during agriculture niche adaptation.

Origin, evolution, and distribution of the molecular machinery for biosynthesis of sialylated lipooligosaccharide structures in Campylobacter coli