In vitro binding of Campylobacter jejuni surface proteins to murine small intestinal cell membranes

Surface proteins of nine Campylobacter jejuni strains belonging to three different serovia were extracted with lysozyme/ethylenediamine-tetraacetic acid. The preparations bound to isolated murine small intestinal cells and to a membrane fraction (MF) of isolated brush borders obtained by detergent treatment with Triton X-100 and Nonidet P40. Binding was demonstrated by an enzyme-linked immunosorbent assay procedure. Using lipopolysaccharide (LPS)- and flagella-specific antisera the contribution of flagella and LPS, present in the protein preparations, to the total binding to MF was investigated. Only up to approximately 10% of the total binding of each strain was found to be mediated by LPS, 10%-33% of binding was flagella dependent. The preparations of four strains (serovar HS2) bound in a trypsin-sensitive manner (45%-85% reduction), while the others (serovaria HS1 and HS13) were hardly influenced by trypsin treatment. Binding to MF was not impaired by preincubation of the bacterial surface protein preparations with several sugars and lectins.