Identification of a 29 kDa flagellar sheath protein in Helicobacter pylori using a murine monoclonal antibody.
The membrane-like flagellar sheath of Helicobacter pylori is of unknown function and little is known of its composition. A murine monoclonal antibody to H. pylori, designated GF6, which reacts by immunoblot with a polypeptide with an apparent molecular mass of 29 kDa was shown by immunogold-electron microscopy to label specifically the flagellar sheath structure. The antigen was detected by immunoblot using the monoclonal antibody in all 11 strains, of diverse geographic origin, so far tested. The antibody also reacted weakly with polypeptides with apparent molecular masses of 65 kDa in Vibrio cholerae and Vibrio parahaemolyticus. The antigen was shown by one- and two-dimensional electrophoretic analysis and immunoblotting to be distinct from the abundant urease subunit UreA, of similar molecular mass. Identification of this flagellar sheath polypeptide will facilitate investigation of the structure and function of the flagellar sheath of this important gastric pathogen.[1]References
- Identification of a 29 kDa flagellar sheath protein in Helicobacter pylori using a murine monoclonal antibody. Luke, C.J., Penn, C.W. Microbiology (Reading, Engl.) (1995) [Pubmed]
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