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Extracellular proteins in five clostridial species from human infections

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Abstract

347 strains from human infections were identified by gas-liquid chromatography of metabolic products and by conventional tests. Simple agar-plate assays were used to analyze the ability to form extracellular proteins. More than 90% of all strains were hemolytic on agar containing rabbit erythrocytes and all were gelatinase producers. All strains ofC. bifermentans, C. sordelli, andC. sporogenes were also caseinolytic on skimmed-milk agar, but strains ofC. perfringens, C. novyi types A and B were not. Less than 10% ofC. perfringens strains were producers of elastase and staphylolytic enzyme and all other species were non-producers. AllC. perfringens, C. novyii, C. bifermentans, andC. sordelli were lecithinase producers, butC. sporogenes was not. All strains ofC. sporogenes formed deoxyribonuclease, while a varying number of the other species showed a positive reaction.

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References

  • Allen, P. W.: A simple method for the classification of bacteria as to the diastase production. J. Bact.3, 15–17 (1918)

    Google Scholar 

  • Brooks, M. E., Sterne, M., Warrack, G. H.: A reassessment of the criteria used for type differentiation ofClostridium welchii. J. Path. Bact.74, 185–195 (1957)

    Google Scholar 

  • Brown, M. R. W., Scott, J. H.: A simple diagnostic milk medium forPseudomonas aeruginosa. J. clin. Path.23, 172–177 (1970)

    PubMed  Google Scholar 

  • Collee, J. G.: The relationship of hemagglutinin ofClostridium perfringens to the neuraminidase and their soluble products of the organism. J. Path. Bact.90, 13–30 (1965)

    PubMed  Google Scholar 

  • DiSalvo, I. V.: Deoxyribonuclease and coagulase activity of Micrococcia. Med. Tech. Bull.9, 191–196 (1958)

    Google Scholar 

  • Dowell, V. R., Hawkins, T. M.: Laboratory methods in anaerobic bacteriology. Center for Disease Control, Atlanta, Georgia; U.S.A. 1968

    Google Scholar 

  • Evans, D. G.: Thein vitro production ofα-toxin,θ-haemolysin and hyaluronidase by strains ofCl. welchii type A and the relationship andin vitro properties to virulence in guinea pigs. J. Path. Bact.57, 75–85 (1945)

    Google Scholar 

  • Finegold, S. M., Marsh, V. H., Bartlett, J. G.: Anaerobic infections in the comprised host. In: Proceedings of the International Conference on Nosocomial Infections. American Hospital Association, Chicago, Ill., p. 123–134 (1971)

    Google Scholar 

  • Finegold, S. M., Rosenblatt, J. G.: Practical aspects on anaerobic sepsis. Medicine (Baltimore)52, 311–322 (1973)

    Google Scholar 

  • Frazier, W. C.: A method for the detection of changes in gelatin due to bacteria. J. infect. Dis.39, 302–309 (1926)

    Google Scholar 

  • Hausken, O. W.: Serological studies on proteolytic enzymes of genusClostridium. Acta path. microbiol. scand.71, 387–392 (1967)

    Google Scholar 

  • Holdeman, L. V., Moore, W. E. C.: Anaerobe laboratory manual. Virginia Polytechnic Institute and State University, Blacksburg, Virginia U.S.A. 1973

    Google Scholar 

  • Hugo, W. B., Beveridge, E. G.: Quantitative and qualitative study of the lipolytic activity of single strains of seven bacterial species. J. appl. Bact.25, 72–82 (1962)

    Google Scholar 

  • MacLennan, J. D.: Histotoxic clostridial infections of man. Bact. Rev.26, 177–276 (1962)

    PubMed  Google Scholar 

  • Mandl, I., Zipper, H., Fenguson, L. T.:Clostridium histolyticum collagenase: its purification and properties. Arch. Biochem. Biophys.74, 465–475 (1958)

    PubMed  Google Scholar 

  • Miller, A., III, Sandine, W. G., Elliker, P. R.: Extracellular nuclease in the genusLactobacillus. J. Bact.108, 604–606 (1971)

    PubMed  Google Scholar 

  • Moore, W. E. C., Cato, E. P., Holdeman, L. V.: Anaerobic bacteria of the gastrointestinal flora and their occurrence in clinical infections. J. infect. Dis.119, 641–649 (1969)

    PubMed  Google Scholar 

  • Moss, C. W., Schecter, K. F., Charry, W. B.: Distribution of the neuraminidase among food poisoning strains ofC. perfringens. Appl. Microbiol..15, 718–722 (1967)

    PubMed  Google Scholar 

  • Möllby, R., Wadström, T.: Purification of phospholipase C (α toxin) fromClostridium perfringens. Biochim. biophys. Acta (Amst.)321, 569–584 (1973)

    Google Scholar 

  • Nord, C.-E., Wadström, T.: Characterization of haemolytic enterococci isolated from oral infections. Acta odont. scand.31, 387–393 (1973)

    PubMed  Google Scholar 

  • Nord, C.-E., Möllby, R., Smyth, C., Wadström, T.: Formation of phospholipase C andθ-haemolysin in pre-reduced media in batch and continuous culture ofClostridium perfingens type A. J. gen. Microbiol.84, 117–127 (1974)

    PubMed  Google Scholar 

  • Oakley, C. L., Warrack, G. H., van Heyningen, W. E.: The collagenase (K-toxin) ofClostridium perfringens type A. J. path. Bact.58, 229–235 (1946)

    Google Scholar 

  • Oakley, C. L., Warrack, G. H.: The ACRA test as a means of estimating hyaluronidase, deoxyribonuclease and their antibodies. J. Path. Bact.63, 45–55 (1951)

    PubMed  Google Scholar 

  • Owens, J. J.: The egg yolk reaction produced by several species by bacteria. J. appl. Bact.37, 137–148 (1974)

    Google Scholar 

  • Princewill, T. J. T., Oakley, C. L.: The deoxyribonucleases and hyaluronidases ofClostridium septicum andC. chauvoei. I. An agar plate method for testing deoxyribonuclease. Med. Lab. Technol.29, 243–354 (1972a)

    PubMed  Google Scholar 

  • Princewill, T. J. T., Oakley, C. L.: The deoxyribonucleases and hyaluronidases ofClostridium septicum andC. chauvoei. II. An agar plate method for testing hyaluronidase. Med. Lab. Technol.29, 255–260 (1972b)

    PubMed  Google Scholar 

  • Rutter, J. M., Collee, J. G.: Studies on the soluble antigens ofClostridium oedematiens (C. novyi). J. med. Microbiol.2, 395–417 (1969)

    PubMed  Google Scholar 

  • Sbarra, A. J., Gilfillan, R. E., Bardawil, W. A.: A plate assay for elastase activity. Nature (Lond.)188, 322–323 (1960)

    Google Scholar 

  • Smith, L. D. S., Holdeman, L. V.: The pathogenic anaerobic Bacteria. Springfield, Ill.: Ch. C. Thomas 1968

    Google Scholar 

  • Smith L. D. S.: The clostridia. In: Handbook of microbiology, vol. I., pp. 89–96, A.I. Laskin and H. A. Lechavlier, eds. Cleveland, Ohio: CRC Press 1973

    Google Scholar 

  • Smith, R. F., Wilett, N. P.: Rapid plate method for screening hyaluronidase and chondroitin sulphatase-producing microorganisms. Appl. Microbiol.16, 1434–1436 (1968)

    PubMed  Google Scholar 

  • Wadström, T., Hisatsune, K.: Bacteriolytic enzymes fromStaphylococcus aureus. Purification of an endo-Β-N-acetylglucosaminidase. Biochem. J.120, 725–735 (1970)

    PubMed  Google Scholar 

  • Willis, A. T.: Clostridia of wound infection. London: Butterworth 1969

    Google Scholar 

  • Willis, A. T.: Some infections due to anaerobic sporeforming bacteria. In: Anaerobic bacteria. pp. 195–217. A. Balows, R. M. Dehaan, L. B. Guze and V. R. Dowell, eds. Springfield, Ill.: Ch. C. Thomas. 1974

    Google Scholar 

  • Wretlind, B., Hedén, L., Sjöberg, L., Wadström, T.: Production of enzymes and toxins by hospital strains ofPseudomonas aeruginosa in relation to serotype and phagetyping pattern. J. med. Microbiol.6, 91–100 (1973)

    PubMed  Google Scholar 

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Nord, C.E., Wadström, T., Dornbusch, K. et al. Extracellular proteins in five clostridial species from human infections. Med Microbiol Immunol 161, 145–154 (1975). https://doi.org/10.1007/BF02121004

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