Nippon Saikingaku Zasshi

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We prepared live and killed antigens of Babesia gibsoni for serological and immunological studies. The serum-antibody titers of the dogs infected with B. gibsoni and immunized with killed B. gibsoni were determined by the indirect fluorescent antibody (IFA) test.
Of the 14 dogs experimentally infected with B. gibsoni, 10 survived and showed significant increase in the IFA titer to B. gibsoni (1:3, 200 in 3 to 4 weeks and 1:12, 800 in 2 months after the infection). The other four dogs died of babesiosis showing little increase in the IFA titer (1:80∼1:800 in 3 weeks after infection).
When live B. gibsoni was reinoculated into two dogs having survived the infection with IFA titers of 1:12, 800, no erythroparasitemia was observed and B. gibsoni disappeared in 2 weeks after the reinoculation. The IFA titers of over 1:12, 800 persisted during the observation period. We thought that such a high IFA titer prevented the dogs from infection with B. gibsoni.
Four healthy dogs were immunized twice with killed B. gibsoni at a 3 week interval, and then challenged with live B. gibsoni in 3 weeks after the second immunization. It took 2 weeks for the IFA titer to increase gradually after the first immunization and titers of 1:400∼1:800 were maintained after the second immunization. All of them survived the challenge and the IFA titers rapidly increased to 1:12, 800. Parasitemia on a low level was observed. The immunization with killed B. gibsoni antigen protected the dogs against babesiosis (erythroparasitemia, splenomegaly) in comparison with the non-immunized group.

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The tetragonally arrayed macromolecular structure in the cell wall of Bacillus aneurinolyticus (Kimura et Aoyama) S232 was isolated and characterized.
The cell wall of B. aneurinolyticus KA was prepared by sonication, differential centrifugation, nuclease treatment, Triton X-100 treatment and washed with water. The regularly arrayed particles were extracted from the purified cell wall preparation with 2M guanidine hydrochloride or 6M urea. SDS-PAGE revealed that the particle of the regular array was a single glycopolypeptide of a molecular weight of 129, 000. The polypeptide contained all amino acids, that were classified into hydrophobic, 39.2% (mole %); neutral, 26.5%; acidic, 21.1%; and basic amino acids, 13.2%. These data indicated the acidic nature of the polypeptide. Its UV absorption spectra in either 6M guanidine hydrochloride or distilled water showed a typical curve of polypeptide with absorption maxima at 277nm and 279nm and an absorption minimum at 250nm in water.
The regularly arrayed particles in B. aneurinolyticus KA were compared in the properties with those of other bacterial strains.

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