Skip to main content
Infection and Immunity logoLink to Infection and Immunity
. 1992 Jul;60(7):3002–3006. doi: 10.1128/iai.60.7.3002-3006.1992

Morphological and biochemical study of cytoskeletal changes in cultured cells after extracellular application of Clostridium novyi alpha-toxin.

A Oksche 1, R Nakov 1, E Habermann 1
PMCID: PMC257267  PMID: 1612767

Abstract

Clostridium novyi alpha-toxin caused retraction and rounding of cultured endothelial cells from porcine pulmonary arteries; nevertheless, the endothelial cells firmly adhered to their supports. F-actin stained with fluorescein-labeled phalloidin was condensed around the nucleus, whereas intermediate filaments and microtubules appeared unchanged. The content of F-actin and myosin was decreased, but that of G-actin or vimentin was not. A predominant role of the microfilament system in C. novyi alpha-toxin cytopathic action is suggested.

Full text

PDF
3002

Images in this article

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Bette P., Frevert J., Mauler F., Suttorp N., Habermann E. Pharmacological and biochemical studies of cytotoxicity of Clostridium novyi type A alpha-toxin. Infect Immun. 1989 Aug;57(8):2507–2513. doi: 10.1128/iai.57.8.2507-2513.1989. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Bette P., Oksche A., Mauler F., von Eichel-Streiber C., Popoff M. R., Habermann E. A comparative biochemical, pharmacological and immunological study of Clostridium novyi alpha-toxin, C. difficile toxin B and C. sordellii lethal toxin. Toxicon. 1991;29(7):877–887. doi: 10.1016/0041-0101(91)90224-f. [DOI] [PubMed] [Google Scholar]
  3. Blikstad I., Markey F., Carlsson L., Persson T., Lindberg U. Selective assay of monomeric and filamentous actin in cell extracts, using inhibition of deoxyribonuclease I. Cell. 1978 Nov;15(3):935–943. doi: 10.1016/0092-8674(78)90277-5. [DOI] [PubMed] [Google Scholar]
  4. Drenckhahn D., Dermietzel R. Organization of the actin filament cytoskeleton in the intestinal brush border: a quantitative and qualitative immunoelectron microscope study. J Cell Biol. 1988 Sep;107(3):1037–1048. doi: 10.1083/jcb.107.3.1037. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Fiorentini C., Arancia G., Paradisi S., Donelli G., Giuliano M., Piemonte F., Mastrantonio P. Effects of Clostridium difficile toxins A and B on cytoskeleton organization in HEp-2 cells: a comparative morphological study. Toxicon. 1989;27(11):1209–1218. doi: 10.1016/0041-0101(89)90029-9. [DOI] [PubMed] [Google Scholar]
  6. Fiorentini C., Malorni W., Paradisi S., Giuliano M., Mastrantonio P., Donelli G. Interaction of Clostridium difficile toxin A with cultured cells: cytoskeletal changes and nuclear polarization. Infect Immun. 1990 Jul;58(7):2329–2336. doi: 10.1128/iai.58.7.2329-2336.1990. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Fiorentini C., Thelestam M. Clostridium difficile toxin A and its effects on cells. Toxicon. 1991;29(6):543–567. doi: 10.1016/0041-0101(91)90050-2. [DOI] [PubMed] [Google Scholar]
  8. Hatheway C. L. Toxigenic clostridia. Clin Microbiol Rev. 1990 Jan;3(1):66–98. doi: 10.1128/cmr.3.1.66. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Heacock C. S., Bamburg J. R. The quantitation of G- and F-actin in cultured cells. Anal Biochem. 1983 Nov;135(1):22–36. doi: 10.1016/0003-2697(83)90725-x. [DOI] [PubMed] [Google Scholar]
  10. Kushnaryov V. M., Sedmak J. J. Effect of Clostridium difficile enterotoxin A on ultrastructure of Chinese hamster ovary cells. Infect Immun. 1989 Dec;57(12):3914–3921. doi: 10.1128/iai.57.12.3914-3921.1989. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Malorni W., Fiorentini C., Paradisi S., Giuliano M., Mastrantonio P., Donelli G. Surface blebbing and cytoskeletal changes induced in vitro by toxin B from Clostridium difficile: an immunochemical and ultrastructural study. Exp Mol Pathol. 1990 Jun;52(3):340–356. doi: 10.1016/0014-4800(90)90074-n. [DOI] [PubMed] [Google Scholar]
  12. Markwell M. A., Haas S. M., Bieber L. L., Tolbert N. E. A modification of the Lowry procedure to simplify protein determination in membrane and lipoprotein samples. Anal Biochem. 1978 Jun 15;87(1):206–210. doi: 10.1016/0003-2697(78)90586-9. [DOI] [PubMed] [Google Scholar]
  13. Mitchell M. J., Laughon B. E., Lin S. Biochemical studies on the effect of Clostridium difficile toxin B on actin in vivo and in vitro. Infect Immun. 1987 Jul;55(7):1610–1615. doi: 10.1128/iai.55.7.1610-1615.1987. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Ottlinger M. E., Lin S. Clostridium difficile toxin B induces reorganization of actin, vinculin, and talin in cultured cells. Exp Cell Res. 1988 Jan;174(1):215–229. doi: 10.1016/0014-4827(88)90156-5. [DOI] [PubMed] [Google Scholar]
  15. Rees M. K., Young M. Studies on the isolation and molecular properties of homogeneous globular actin. Evidence for a single polypeptide chain structure. J Biol Chem. 1967 Oct 10;242(19):4449–4458. [PubMed] [Google Scholar]
  16. Reuner K. H., Presek P., Boschek C. B., Aktories K. Botulinum C2 toxin ADP-ribosylates actin and disorganizes the microfilament network in intact cells. Eur J Cell Biol. 1987 Feb;43(1):134–140. [PubMed] [Google Scholar]
  17. Schnittler H. J., Wilke A., Gress T., Suttorp N., Drenckhahn D. Role of actin and myosin in the control of paracellular permeability in pig, rat and human vascular endothelium. J Physiol. 1990 Dec;431:379–401. doi: 10.1113/jphysiol.1990.sp018335. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. Shahrabadi M. S., Bryan L. E., Lee P. W. Interaction of Clostridium difficile toxin A with L cells in culture. Can J Microbiol. 1984 Jul;30(7):874–883. doi: 10.1139/m84-137. [DOI] [PubMed] [Google Scholar]

Articles from Infection and Immunity are provided here courtesy of American Society for Microbiology (ASM)

RESOURCES