Isolation and characterization of bacterial flagellar hook proteins from salmonellae and Escherichia coli.
Flagellar hook proteins from Salmonella and Escherichia coli were dissociated in acid and purified by diethylamino-ethyl-cellulose column chromatography. These two proteins had the same electrophoretic mobility in sodium dodecyl sulfate-polyacrylamide gels. However, analytical electrofocusing patterns showed that these proteins had different isoelectric points (4.7 for Salmonella typhimurium and 4.4 for E. coli). Immunodiffusion and immuno-electron microscopy carried out with antisera prepared against purified hook proteins from S. typhimurium and E. coli showed that these antisera reacted with both hooks. Affinity chromatography allowed separation of antibodies specific for hook proteins from each bacterial species. These results indicate that the hook proteins share common antigenic determinants as well as specific antigens, although the specificity is not quantitatively resolved. From comparisons of the amino acid composition of the hook proteins and flagellins, it was concluded that the differences between flagellins from S. typhimurium and E. coli were larger than those between hook proteins from these species.
D000907:Antibodies, Bacterial; D001426:Bacterial Proteins / Q000032:analysis* / Q000276:immunology; D004926:Escherichia coli / Q000032:analysis*; D005407:Flagella / Q000032:analysis*; D005779:Immunodiffusion; D007526:Isoelectric Point; D008854:Microscopy, Electron; D012475:Salmonella / Q000032:analysis*; D012486:Salmonella typhimurium / Q000032:analysis*
D000907:Antibodies, Bacterial; D001426:Bacterial Proteins