A possibility of application of the 105-kilodaltons protein of Brachyspira alvinipulli cross-reacting with antisera to five species in the genus Brachyspira to diagnosis

The antigenic properties of Brachyspira (B.) alvinipulli ATCC 51933 and strain C2 were analyzed and compared with those of B. hyodysenteriae ATCC 27164 and ATCC 31212. B. pilosicoli ATCC 51139. B. innocens ATCC 29796 and B. aalborgi NCTC 11492. In gel immunodiffusion tests, a protein in B. alvinipul...

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Veröffentlicht in:Journal of Veterinary Medical Science 2004, Vol.66(7), pp.773-778
Hauptverfasser: Abe, Y. (Ibaraki Univ., Ami (Japan). Coll. of Agriculture), Adachi, Y
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Sprache:eng
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Zusammenfassung:The antigenic properties of Brachyspira (B.) alvinipulli ATCC 51933 and strain C2 were analyzed and compared with those of B. hyodysenteriae ATCC 27164 and ATCC 31212. B. pilosicoli ATCC 51139. B. innocens ATCC 29796 and B. aalborgi NCTC 11492. In gel immunodiffusion tests, a protein in B. alvinipulli ATCC 51933 reacted strongly with anti-B.. alvinipulli ATCC 51933serum and formed two precipitin lines. Furthermore, by an immunoblotting technique, the 105-kilodaltons (kDa) protein in B. alvinipulli ATCC 51933 reacted strongly with each of the antisera to B. hyodysenteriae, B. pilosicoli, B. innocens and B. aalborgi. Therefore, the 105-kDa protein could be applied to diagnosis of chicken infection by B. alvinipulli and B. pilosicoli. But the 105-kDa protein reacting with the anti-fl. alvinipulli ATCC 51933-serum was not confirmed in B. hyodysenteriae. B. pilosicoli, B. innocens and B. aalborgi. The N-terminal amino acid sequence of the 105-kDa protein isolated from B. alvinipulli ATCC 51933 was Met-Lys-Lys-Met-Val-Tyr-Phe-Phe-Gly-Asn. The amino acid alignment of this protein possessed 50% homology with the periplasmic-iron-binding protein BitC in B. hyodysenteriae.
ISSN:0916-7250
1347-7439
DOI:10.1292/jvms.66.773