ISOLATION AND CHARACTERIZATION OF THE FLAGELLAR HOOK OF CAMPYLOBACTER-JEJUNI

A method for purification of the flagellar hook of Campylobacter jejun i is described. The hook was shown to be composed of a subunit protein , which has a molecular mass of 92,000 and an isoelectric point of pI 4.8. A monoclonal antibody and a polyvalent antiserum was raised again st the purified flagellar hook of C. jejuni. Immuno-electronmicroscopy revealed that the epitope recognized by the monoclonal antibody is su rface-located. However, this antibody reacted only with the hook of th e immunization strain, but not with other strains or other flagellated bacteria. Thus, our data indicate that the immunodominant epitopes ar e located on the surface of the hook and that these epitopes are strai n-specific.