Open AccessIsolation and characterization of the flagellar hook of Campylobacter jejuni
Author(s) -
GlennCalvo Eduardo,
Bär Werner,
Frosch Matthias
Publication year - 1994
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.1994.tb07228.x
Subject(s) - epitope , campylobacter jejuni , antiserum , monoclonal antibody , isoelectric point , microbiology and biotechnology , strain (injury) , hook , biology , flagellum , antibody , protein subunit , campylobacter , isolation (microbiology) , bacteria , chemistry , biochemistry , enzyme , anatomy , genetics , medicine , dentistry , gene
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.