The periplasmic flagella of Serpulina (Treponema) hyodysenteriae are composed of two sheath proteins and three core proteins.
The major components of the periplasmic flagella of the spirochaete Serpulina (Treponema) hyodysenteriae strain C5 were purified and characterized. We demonstrate that the periplasmic flagella are composed of five major proteins (molecular masses 44, 37, 35, 34 and 32 kDa) and present their location, N-terminal amino acid sequence and immunological relationship. The 44 kDa and the 35 kDa protein are on the sheath of the periplasmic flagellum, whereas the 37, 34 and 32 kDa protein reside in the periplasmic flagellar core. The two sheath flagellar proteins are immunologically related but have different N-terminal amino acid sequences. The N-terminus of the 44 kDa protein shows homology with the sheath flagellins of other spirochaetes, but the 35 kDa protein does not. The three core proteins are immunologically cross-reactive and their N-terminal amino acid sequences are almost, but not completely, identical, indicating that the core proteins are encoded by three distinct genes. The core proteins show extensive N-terminal sequence similarities and an immunological relationship with periplasmic flagellar core proteins of other spirochaetes.
Koopman
M B
MB
Department of Bacteriology, School of Veterinary Medicine, University of Utrecht, The Netherlands.
Baats
E
E
van Vorstenbosch
C J
CJ
van der Zeijst
B A
BA
Kusters
J G
JG
D000595:Amino Acid Sequence; D000942:Antigens, Bacterial; D015153:Blotting, Western; D017401:Brachyspira hyodysenteriae / Q000737:chemistry* / Q000648:ultrastructure; D017124:Conserved Sequence; D005407:Flagella / Q000737:chemistry* / Q000648:ultrastructure; D005408:Flagellin / Q000737:chemistry* / Q000302:isolation & purification; D007150:Immunohistochemistry; D016253:Microscopy, Immunoelectron; D008969:Molecular Sequence Data; D008970:Molecular Weight; D017386:Sequence Homology, Amino Acid; D013144:Spirochaetales / Q000737:chemistry
D000942:Antigens, Bacterial; D005408:Flagellin