Recovery of spirochagetes in the monkey by passive transfer from human late sero-negative syphilis.
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Spirochaetes isolated from field samples of diarrhoea, 'colitis' and mucoid diarrhoea from pigs were examined by a series of cultural, biochemical and serological tests. In addition sodium dodecyl sulphate polyacrylamide gel electrophoresis was used to determine whether the organisms possessed a 16 kDa protein thought to distinguish Serpulina hyodysenteriae from S innocens. Spirochaetal isolates which differed culturally and biochemically from S hyodysenteriae were found to possess a 16 kDa protein. One of these isolates was examined by electron microscopy and found to have an ultrastructure differing from that of S hyodysenteriae. Antiserum to the 16 kDa antigen of S hyodysenteriae reacted with isolate S80/5, the homologous strain, and with B78, the type species, but not with the 16 kDa antigens of the field isolates considered to be S hyodysenteriae or with the non-S hyodysenteriae spirochaetes. It was concluded that there may be a family of 16 kDa proteins located on the envelope of various spirochaetes responsible for diarrhoea in pigs.
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The lipid compositions of two spirochetes isolated from the human oral cavity and two isolated from pig feces were examined. These isolates were unusual in that they did not require long-chain fatty acids for growth, as do the other host-associated spirochetes, but rather required isobutyric and valeric acids. Therefore, they could be cultured in a medium free of serum or fatty acid - albumin supplements. The major fatty acids synthesized were normal and iso fatty acids with 14 and 16 carbons. No unsaturated fatty acids were detected, nor were chain lengths longer than 16 carbons. The major complex lipids found were monogalactosyl diglyceride, phosphatidyl glycerol, and bis-phosphatidyl glycerol. Nitrogenous phospholipids, present in Treponema and Leptospira, were not synthesized by these novel strains. The data indicate an intermediate position of these isolates between Treponema and free-living Spriochaeta.
A free-living spirochete has been found in the activated sludge of purification plants in Amsterdam. A partial enrichment of the spirochete could be obtained with a passage through a thin layer of water agar. The morphology of this spirochetal strain does not fit into one of the described genera in Bergey's Manual. The cells have many regular primary coils on which broad secondary coils are superimposed and the protoplasmic cylinder is tightly wound around an axistyle,
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Although spirochete periplasmic flagella have many features similar to typical bacterial flagella, they are unique in their structure and internal periplasmic location. This location provides advantages for pathogenic spirochetes to enter and to adapt in the appropriate host, and to penetrate through matrices that inhibit the motility of most other bacteria. These flagella are complex, and they dynamically interact with the spirochete cell cylinder in novel ways. Electron microscopy, tomography and three-dimensional reconstructions have provided new insights into flagellar structure and its relationship to the spirochetal cell cylinder. Recent advances in genetic methods have begun to shed light on the composition of the spirochete flagellum, and on the regulation of its synthesis. Because spirochetes have a high length to width ratio, their cells provide an opportunity to study two important features. These include the polarity or distribution of flagellar synthesis as well as the mechanisms required for coordination of the movement of the cell ends, to enable it to move in the forward or reverse direction.
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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 51933-serum 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-B. 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.
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