α1–2 Fucosylated Chains (H-2, H-1, and Lewisb) are the Main Human Milk Receptor Analogs for Campylobacter
The pathogenesis of Campylobacter diarrhoea involves a series of complex events, in which toxin production and adherence and invasion to gut mucosa are of primary importance. A possible strategy for the prevention of gastrointestinal infections is the inhibition of enteropathogen attachment to mucosal surfaces. It has been reported that human milk contributes to the protection against gastrointestinal infections in infants, presumably by acting as receptor analogues for pathogens. To determine the role of factors present in human milk that may act as receptor analogues for C. jejuni, we used isolates from children participating in a cohort study, where the clinical outcome of infection was well defined; we developed an in vitro inhibition assay for bacterial association using HEp-2 cells and 4 oligosaccharide (OS) fractions of human milk, and an experimental model for colonization in mice. Strong inhibition of cell association was observed with the crude OS fractions. When these were further purified, only the neutral fraction retained inhibitory activity, and, when further purified, only the fucosylated OS were inhibitory. To identify the fucose-containing determinants that inhibited the attachment of Campylobacter in vitro and in vivo, we developed two bacterial-binding assays, a Western blot and an ELISA, with a group of commercially available fucosylated carbohydrate chains linked to proteins. With these methods we were able to characterize three main human milk receptor analogs that inhibited Campylobacter attachment to epithelial cells.
KeywordsHuman Milk Gastrointestinal Infection Neutral Fraction Cell Association Bacterial Association
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