Open AccessIdentification of flagellar and associated polypeptides of Helicobacter (formerly Campylobacter ) pylori
Author(s) -
Luke C.J.,
Kubiak E.,
Cockayne A.,
Elliott T.S.J.,
Penn C.W.
Publication year - 1990
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.1574-6968.1990.tb03827.x
Subject(s) - flagellum , immunogold labelling , flagellin , biology , microbiology and biotechnology , bacterial outer membrane , gel electrophoresis , antiserum , campylobacter jejuni , molecular mass , centrifugation , biochemistry , bacteria , chemistry , ultrastructure , antigen , gene , escherichia coli , anatomy , genetics , enzyme
Flagella of Helicobacter pylori were isolated from intact organisms by shearing and differential centrifugation. Treatment of the flagella with the detergent Triton X‐100 removed the flagellar sheath, which was confirmed by electron microscopy, and the remaining naked flagella were shown by sodium dodecyl sulphate polyacryl amide gel electrophoresis (SDS‐PAGE) to consist primarily of a single 54 kilodalton (kDa) polypeptide. This was confirmed by immunogold labelling and electron microscopy of detergent treated whole organisms, using a mouse antiserum specific for the 54 kDa polypeptide. Polypeptides solubilised from crude flagellar preparations by detergent treatment were found to have molecular weights of 26, 30, 58, 62, 66 and 80 kDa. These polypeptides are possible components of the flagellar sheath and they may represent outer membrane proteins, based on the assumption that the flagellar sheath is related in composition to the outer membrane of the organism. Analysis and definition of these components of the surface structures of the organism are important in understanding the interaction between the organism and its host in pathogenesis.