CAMPYLOBACTER-JEJUNI MAJOR OUTER-MEMBRANE PROTEIN AND A 59-KDA PROTEIN ARE INVOLVED IN BINDING TO FIBRONECTIN AND INT 407 CELL-MEMBRANES

Campylobacter jejuni is one of the major causes of human diarrhea thro ughout the world. Attachment to host cells and extracellular matrix pr oteins is considered to be an essential primary event in the pathogene sis of enteritis. Outer membrane proteins of three C. jejuni strains, one of which was aflagellate, were investigated for their contribution to the process of adhesion to INT 407 cell membranes and the extracel lular matrix protein fibronectin. Using a ligand-binding immunoblottin g assay the flagellin, the major outer membrane protein and a 59-kDa p rotein were detected to be involved in adhesion to both substrates. Th e MOMP was able to inhibit the attachment of the bacteria to INT 407 c ell membranes partly, when the protein was isolated under native condi tions. However, it was totally lost when the protein was isolated in t he presence of SDS. The 59-kDa protein of one strain was identified by N-terminal sequencing, and regarding the first 14 amino acids it was found to be identical to the 37-kDa CadF protein just recently describ ed as fibronectin-binding protein of C. jejuni. Especially for the afl agellate strain this protein may be of special importance for adhesion of the bacteria to different substrates.