Variation in the primary structure of Bacillus subtilis flagellins.
The flagella derived from 18 strains Bacillus subtilis were tested for their reaction with antiflagellar filament antibody and antiflagellin antibody. On the basis of their reactivity, at least five serologically distinct classes could be identified. Peptide map analysis of tryptic digests of the subunit proteins were consistent with the immunochemical analysis. Large differences in sequence existed among proteins of the different classes; proteins within an antigenic group differed by only a few peptides. Furthermore, 9 of the 27 tryptic peptides resolved were common to flagellin proteins from all the classes examined. The relationship between antigenic specificity, variability in peptide pattern, and the conformation of the flagellin protein are discussed.
D000818:Animals; D000937:Antigen-Antibody Reactions; D000942:Antigens, Bacterial / Q000032:analysis; D001412:Bacillus subtilis / Q000032:analysis* / Q000145:classification / Q000276:immunology; D001426:Bacterial Proteins / Q000032:analysis* / Q000302:isolation & purification; D002855:Chromatography, Thin Layer; D003168:Complement Fixation Tests; D003429:Cross Reactions; D004589:Electrophoresis, Disc; D007106:Immune Sera; D007202:Indicators and Reagents; D010455:Peptides / Q000032:analysis*; D011817:Rabbits; D012703:Serotyping; D012964:Sodium; D013431:Sulfates; D014357:Trypsin / Q000378:metabolism
D000942:Antigens, Bacterial; D001426:Bacterial Proteins; D007106:Immune Sera; D007202:Indicators and Reagents; D010455:Peptides; D013431:Sulfates; D012964:Sodium; D014357:Trypsin