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Summary

Biological and biochemical characteristics of the leukotoxin of Fusobacterium necrophorum were determined. Culture supernatant of F necrophorum was toxic to polymorphonuclear neutrophilic, leukocytes from cattle and sheep, but not to those from pigs and rabbits. Culture supernatant and sonicated bacterial cell fractions had low hemolytic activity and did not cause dermonecrosis in a guinea pig. Supernatant derived leukotoxin was inactivated at 56 C for 5 minutes and became unstable at pH > 7.8 or < 6.6. Chemical treatment with 0.1% sodium dodecyl sulfate, 0.25% sodium deoxycholate, 5.2% sodium sulfide, or 0.25 mM titanium (III) citrate markedly decreased leukotoxicity. Enzymatic treatment with protease, trypsin, and chymotrypsin inactivated the toxin completely, whereas amylase had no effect. Use of protease inhibitors failed to prevent loss of leukotoxin activity. Using membrane partition chromatography and gel filtration, the estimated molecular weight of the toxin was > 300,000. On reduction and denaturation, the toxin dissociated into several components by use of sodium dodecyl sulfate-polyacrylamide gel electrophoresis.

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in American Journal of Veterinary Research

SUMMARY

Pili from 11 distinct serotypes of Bacteroides nodosus were examined for diversity of pilin polypeptide subunits among serotypes and for purity of the pilin preparations. The pilin of all 11 samples was shown to be homogeneous. Mean ± sd molecular weight of the pilin of 7 serotypes (A198, IV, V, VI, IX, XVII, and XVIII) was 18,500 ± 100. The pilin of serotypes I, III, and VIII had molecular weight of 17,600, 19,400, and 19,000, respectively. Serotype XV differed greatly from the other 10 serotypes in that 2 distinct polypeptide bands with molecular weight of approximately 7,800 and 6,200 were detected. We suggest that these 2 low molecular weight bands resulted from proteolytic cleavage of the pilin protein.

Free access
in American Journal of Veterinary Research