Skip to main content
Infection and Immunity logoLink to Infection and Immunity
. 1981 Jun;32(3):1187–1192. doi: 10.1128/iai.32.3.1187-1192.1981

Membrane-damaging action of alveolysin from Bacillus alvei.

M Thelestam, J E Alouf, C Geoffroy, R Möllby
PMCID: PMC351577  PMID: 6894743

Abstract

We investigated membrane damage to human diploid, embryonic lung fibroblasts caused by highly purified alveolysin by measuring leakage of cytoplasmic markers and uptake of various metabolites, and we observed a leakage pattern typical of SH-activated cytolysins. However, the mode of membrane interaction resembled the mode of membrane interaction of theta-toxin from Clostridium perfringens rather than that of streptolysin O in the following respects: the activity on fibroblast membranes was high compared with the activity on sheep erythrocytes; the toxin did not bind irreversibly to fibroblast cytoplasmic membranes; considerable membrane damage was caused at 0 degrees C; and inhibition of amino acid uptake occurred in the absence of significant structural membrane damage. These findings imply that data on membrane effects caused by streptolysin O cannot be related indiscriminately to other SH-activated cytolysins. With regard to the mode of membrane interaction, two apparently different groups of SH-activated cytolysins exist.

Full text

PDF
1187

Selected References

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

  1. Alouf J. E., Kiredjian M., Geoffroy C. Purification de l'hémolysine thiol-dépendante extracellulaire de Bacillus alvei. Biochimie. 1977;59(3):329–336. doi: 10.1016/s0300-9084(77)80150-8. [DOI] [PubMed] [Google Scholar]
  2. Alouf J. E., Raynaud M. Action de la streptolysine O sur les membranes cellulaires . II.--Cinétique de la lyse érythrocytaire. Ann Inst Pasteur (Paris) 1968 Jul;115(1):97–121. [PubMed] [Google Scholar]
  3. Alouf J. E., Raynaud M. Action de la streptolysine O sur les membranes cellulaires. I. Fixation sur la membrane érythrocytaire. Ann Inst Pasteur (Paris) 1968 Jun;114(6):812–827. [PubMed] [Google Scholar]
  4. Bernheimer A. W., Grushoff P. Extracellular hemolysins of aerobic sporogenic bacilli. J Bacteriol. 1967 May;93(5):1541–1543. doi: 10.1128/jb.93.5.1541-1543.1967. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Christensen H. N. Amino acid transport systems in animal cells: interrelations and energization. J Supramol Struct. 1977;6(2):205–213. doi: 10.1002/jss.400060206. [DOI] [PubMed] [Google Scholar]
  6. Duncan J. L., Buckingham L. Effects of streptolysin O on transport of amino acids, nucleosides, and glucose analogs in mammalian cells. Infect Immun. 1977 Dec;18(3):688–693. doi: 10.1128/iai.18.3.688-693.1977. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. EAGLE H. Amino acid metabolism in mammalian cell cultures. Science. 1959 Aug 21;130(3373):432–437. doi: 10.1126/science.130.3373.432. [DOI] [PubMed] [Google Scholar]
  8. Eilam Y., Carbantchik I. The mechanism of interaction between high-affinity probes and the uridine transport system of mammalian cells. J Cell Physiol. 1976 Dec;89(4):831–838. doi: 10.1002/jcp.1040890451. [DOI] [PubMed] [Google Scholar]
  9. Lubin M. Intracellular potassium and macromolecular synthesis in mammalian cells. Nature. 1967 Feb 4;213(5075):451–453. doi: 10.1038/213451a0. [DOI] [PubMed] [Google Scholar]
  10. Plagemann P. G. Nucleoside transport by Novikoff rat hepatoma cells glowing in suspension culture. Specificity and mechanism of transport reactions and relationship to nucleoside incorporation into nucleic acids. Biochim Biophys Acta. 1971 Jun 1;233(3):688–701. doi: 10.1016/0005-2736(71)90168-4. [DOI] [PubMed] [Google Scholar]
  11. Thelestam M., Möllby R. Classification of microbial, plant and animal cytolysins based on their membrane-damaging effects of human fibroblasts. Biochim Biophys Acta. 1979 Oct 19;557(1):156–169. doi: 10.1016/0005-2736(79)90098-1. [DOI] [PubMed] [Google Scholar]
  12. Thelestam M., Möllby R. Determination of toxin-induced leakage of different-size nucleotides through the plasma membrane of human diploid fibroblasts. Infect Immun. 1975 Apr;11(4):640–648. doi: 10.1128/iai.11.4.640-648.1975. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Thelestam M., Möllby R. Interaction of streptolysin O from Streptococcus pyogenes and theta-toxin from Clostridium perfringens with human fibroblasts. Infect Immun. 1980 Sep;29(3):863–872. doi: 10.1128/iai.29.3.863-872.1980. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Thelestam M., Möllby R. Sensitive assay for detection of toxin-induced damage to the cytoplasmic membrane of human diploid fibroblasts. Infect Immun. 1975 Aug;12(2):225–232. doi: 10.1128/iai.12.2.225-232.1975. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Walum E., Edström A. Kinetics of 2-deoxy-D-glucose transport into cultured mouse neuroblastoma cells. Exp Cell Res. 1976 Jan;97:15–22. doi: 10.1016/0014-4827(76)90649-2. [DOI] [PubMed] [Google Scholar]

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

RESOURCES