Springer Nature is making SARS-CoV-2 and COVID-19 research free. View research | View latest news | Sign up for updates

Vacuolating, lethal, collagenase and clostripain activities of six reference ATCC Clostridium histolyticum strains

  • 108 Accesses

Abstract

We have previously demonstrated that C. histolyticum reference strain ATCC 19401 produces not only lethal factor but also hitherto unrecognized vacuolating toxin. The aim of this study was to compare vacuolating and lethal activities of six reference C. histolyticum strains (ATCC 6282, 8034, 17859, 17860, 19401 and 25770) and to determine whether production of vacuolating toxin is strain-dependent and how the amounts of both toxins produced by the same strain are related to each other and also to protease, collagenase and clostripain activities. All strains produced vacuolating and lethal toxins as well as collagenase, clostripain and proteases, but with different yield. Strain ATCC 19401 demonstrated considerable vacuolating and lethal activities and low activity of collagenase, clostripain and proteases. In other strains such relationship was not evident. Positive correlations were observed in collagenase and clostripain activities of all studied C. histolyticum strains (r = 0.71). Positive correlations were detected also in vacuolating activities of studied strains and clostripain (r = 0.62) and collagenase (r = 0.87) production, and this effect was statistically significant (P < 0.05). Negative non-significant correlations were detected: (a) in lethal activities of studied strains and clostripain, or collagenase activities, (b) in vacuolating activities and protease production.

This is a preview of subscription content, log in to check access.

Fig. 1
Fig. 2
Fig. 3

References

  1. Berman S, Lowenthal JP, Webster ME, Altieri PL, Gochenour RB (1961) Factors affecting the elaboration by Clostridium histolyticum of proteinases capable of debriding third degree burn eschars on guinea pigs. J Bacteriol 82:582–588

  2. Bicsak TA, Harper E (1985) Purification of non-specific protease-free collagenase from Clostridium histolyticum. Anal Biochem 145:286–291

  3. Bowen HE (1952) A comparison of the lethal and haemolytic toxins of Clostridium histolyticum. Yale J Biol Med 25:131–138

  4. de Bernard M, Moschioni M, Papini E, Telford J, Rappuoli R, Montecucco C (1998) Cell vacuolization induced by Helicobacter pylori vac A toxin: cell line sensitivity and quantitative estimation. Toxicol Lett 99:109–115

  5. Finegold SM, Song Y, Liu C, Hecht DW, Summanen P, Kononen E, Allen SD (2005) Clostridium clostridiforme: a mixture of three clinically important species. Eur J Clin Microbiol Infect Dis 24:319–324

  6. Flick DA, Gifford GE (1984) Comparison of in vitro cell cytotoxic assays for tumor necrosis factor. J Immunol Methods 68:167–175

  7. Giles AM, Imhoff JM, Keil B (1979) Alpha-clostripain. Chemical characterization, activity, and thiol content of the highly active form of clostripain. J Bacteriol 254:1462–1468

  8. Jankowska-Steifer E, Jóźwiak J, Grzela T, Komar A, Niderla J, Łazarczyk M, Korczak-Kowalska G, Moskalewski S, Martirosian G (2006) Vacuolation of HeLa cells by a partially purified Clostridium histolyticum cytotoxin. FEMS Immunol Med Microbiol 46:360–366

  9. Jóźwiak J, Komar A, Jankowska E, Martirosian G (2006) Inhibition of Clostridium histolyticum supernatant cytotoxic activity by protease inhibitors. Enzyme Microb Technol 39:29–31

  10. Jóźwiak J, Jankowska-Steifer E, Grzela T, Komar A, Moskalewski S, Martirosian G (2007) Lethal factor of Clostridium histolyticum kills cells by apoptosis. FEMS Immunol Med Microbiol 49:296–303

  11. Kessler E, Yaron A (1973) A novel aminopeptidase from Clostridium histolyticum. Biochem Biophys Res Commun 50:405–412

  12. Kono T (1968) Purification and partial characterization of collagenolytic enzymes from Clostridium histolyticum. Biochemistry 7:1106–1114

  13. Mandl I, Ferguson LT, Zaffuto SF (1957) Exopeptidases of Clostridium histolyticum. Arch Biochem Biophys 69:565–581

  14. Mitchell WM, Harrington WF (1968) Purification and properties of clostridiopeptidase B (clostripain). J Biol Chem 243:4683–4692

  15. Mookhtiar KA, van Wart HE (1992) Clostridium histolyticum collagenase: a new look at some old enzymes. Matrix Suppl 1:116–126

  16. Moskalewski S, Sochańska KR, Wiwatowski T (1973) The presence of a factor toxic to pancreatic beta cells in some collagenase preparations. Bull Acad Pol Sci 22(2):127–130

  17. Nishida S, Imaizumi M (1966) Toxigenicity of Clostridium histolyticum. J Bacteriol 91:477–483

  18. Oakley CL, Warrack GH (1950) The alpha, beta and gamma antigens of Costridium histolyticum. J Gen Microbiol 4:365–373

  19. Pasternack JG, Bengtson IA (1940) The experimental pathological changes produced by the toxin of Clostridium histolyticum in animals. Pub Health Rep Wash 55:775–784

  20. Porter W, Cunningham L, Mitchell W (1971) Studies on the active site of clostripain. The specific inactivation by the chloromethyl ketone derived from a-N-Tosyl-L- Lysine. J Biol Chem 246:7675–7682

  21. Schallehn G, Wolff HW (1988) Morphologische veränderungen humaner embryonaler lungfibroblasten durch cytotoxine verschiedener clostridium- species. Zbl Bakt Hyg A 267:367–378

  22. Shamraeva SA, Vlasova EV, Shemanova GF, Pyleva ZA (1967) Determination of the activity of Clostridium histolyticum toxins in tissue cultures (in Russian). J Microbiol 5:102–105

  23. Shemanova GF, Vlasova EV, Shamraeva SA (1967) Obtaining of highly purified preparations of a-lethal factor from Clostridium histolyticum (in Russian). Met Bioch Iss 3:632–635

  24. Sparrow LG, McQuade AB (1973) Isolation by affinity chromatography of neutral proteinase from Clostridium histolyticum. Biochim Biophys Acta 302:90–94

  25. Steward SE (1936) Studies on the production of toxin by Clostridium histolyticum. Pub Health Rep Wash 51:1272–1279

  26. Takahashi S, Seifter S, Binder M (1970) Elastolytic activities of Clostridium histolyticum. Biochem Biophys Res Commun 39:1058–1064

  27. Twining SS (1984) Fluorescein isothiocyanate-labeled casein assay for proteolytic enzymes. Anal Biochem 142:30–34

  28. Ullmann D, Jakubke HD (1994) The specificity of clostripain from Clostridium histolyticum. Mapping the S’subsites via acetyl transfer to amino acid amides and peptides. Eur J Biochem 223:865–872

  29. Vlasova YV, Tsurikov FF (1966) Production of a lethal toxin and C. histolyticum collagenase on casein nutritive media. Zhurnal Mikrobiologii, Epidemiologiii Immunobiologii 1:112–114 (technical translation FSTC-HT-23-512-68)

  30. Weinberg M, Séguin P (1916) Contribution à L’étiologie de la gangrene gazeuse. CR Acad Sci Paris 163:449–451

  31. Yoshihara K, Matsushita O, Minami J, Okabe A (1994) Cloning and nucleotide sequence analysis of the col. H gene from Clostridium histolyticum encoding a collagenase and a gelatinase. J Bacteriol 176:6489–6496

Download references

Acknowledgments

This work was supported by a grant from the Polish Ministry of Scientific Research and Information Technology Nr 40404132/0949.

Author information

Correspondence to Gayane Martirosian.

Rights and permissions

Reprints and Permissions

About this article

Cite this article

Jankowska-Steifer, E., Martirosian, G., Ekiel, A. et al. Vacuolating, lethal, collagenase and clostripain activities of six reference ATCC Clostridium histolyticum strains. World J Microbiol Biotechnol 27, 1689–1694 (2011). https://doi.org/10.1007/s11274-010-0623-0

Download citation

Keywords

  • Clostridium histolyticum
  • Toxins
  • Collagenase
  • Clostripain
  • Proteases