Isolation and characterization of the flagellar hook of Campylobacter jejuni.
A method for purification of the flagellar hook of Campylobacter jejuni 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 against the purified flagellar hook of C. jejuni. Immuno-electronmicroscopy revealed that the epitope recognized by the monoclonal antibody is surface-located. However, this antibody reacted only with the hook of the immunization strain, but not with other strains or other flagellated bacteria. Thus, our data indicate that the immunodominant epitopes are located on the surface of the hook and that these epitopes are strain-specific.
Glenn-Calvo
E
E
Institute für Medizinische Mikrobiologie, Medizinische Hochschule Hannover, FRG.
Bär
W
W
Frosch
M
M
D000911:Antibodies, Monoclonal; D001431:Bacteriological Techniques; D016123:Campylobacter jejuni / Q000648:ultrastructure*; D000939:Epitopes / Q000302:isolation & purification; D005407:Flagella / Q000737:chemistry* / Q000276:immunology / Q000648:ultrastructure; D008854:Microscopy, Electron; D016253:Microscopy, Immunoelectron
D000911:Antibodies, Monoclonal; D000939:Epitopes