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. 1990 Dec;172(12):7301–7305. doi: 10.1128/jb.172.12.7301-7305.1990

Alveolysin, the thiol-activated toxin of Bacillus alvei, is homologous to listeriolysin O, perfringolysin O, pneumolysin, and streptolysin O and contains a single cysteine.

C Geoffroy 1, J Mengaud 1, J E Alouf 1, P Cossart 1
PMCID: PMC210863  PMID: 2254290

Abstract

The gene coding for alveolysin, the thiol-activated toxin produced by Bacillus alvei, has been cloned by means of an oligonucleotide based on the known N-terminal sequence of the secreted protein. The complete nucleotide sequence of the gene has been determined. The deduced amino acid sequence of alveolysin shows that alveolysin shares homologies with listeriolysin O, perfringolysin O, pneumolysin, and streptolysin O. Alveolysin, like the other members of the family, contains a single cysteine in the conserved peptide sequence ECTGLA WEWWR.

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Selected References

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  1. Bernheimer A. W., Rudy B. Interactions between membranes and cytolytic peptides. Biochim Biophys Acta. 1986 Jun 12;864(1):123–141. doi: 10.1016/0304-4157(86)90018-3. [DOI] [PubMed] [Google Scholar]
  2. Bhakdi S., Tranum-Jensen J., Sziegoleit A. Mechanism of membrane damage by streptolysin-O. Infect Immun. 1985 Jan;47(1):52–60. doi: 10.1128/iai.47.1.52-60.1985. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Bielecki J., Youngman P., Connelly P., Portnoy D. A. Bacillus subtilis expressing a haemolysin gene from Listeria monocytogenes can grow in mammalian cells. Nature. 1990 May 10;345(6271):175–176. doi: 10.1038/345175a0. [DOI] [PubMed] [Google Scholar]
  4. Cossart P., Mengaud J. Listeria monocytogenes. A model system for the molecular study of intracellular parasitism. Mol Biol Med. 1989 Oct;6(5):463–474. [PubMed] [Google Scholar]
  5. Cossart P., Vicente M. F., Mengaud J., Baquero F., Perez-Diaz J. C., Berche P. Listeriolysin O is essential for virulence of Listeria monocytogenes: direct evidence obtained by gene complementation. Infect Immun. 1989 Nov;57(11):3629–3636. doi: 10.1128/iai.57.11.3629-3636.1989. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Domann E., Chakraborty T. Nucleotide sequence of the listeriolysin gene from a Listeria monocytogenes serotype 1/2a strain. Nucleic Acids Res. 1989 Aug 11;17(15):6406–6406. doi: 10.1093/nar/17.15.6406. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Gaillard J. L., Berche P., Mounier J., Richard S., Sansonetti P. In vitro model of penetration and intracellular growth of Listeria monocytogenes in the human enterocyte-like cell line Caco-2. Infect Immun. 1987 Nov;55(11):2822–2829. doi: 10.1128/iai.55.11.2822-2829.1987. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Gaillard J. L., Berche P., Sansonetti P. Transposon mutagenesis as a tool to study the role of hemolysin in the virulence of Listeria monocytogenes. Infect Immun. 1986 Apr;52(1):50–55. doi: 10.1128/iai.52.1.50-55.1986. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Geoffroy C., Alouf J. E. Interaction of alveolysin A sulfhydryl-activated bacterial cytolytic toxin with thiol group reagents and cholesterol. Toxicon. 1982;20(1):239–241. doi: 10.1016/0041-0101(82)90208-2. [DOI] [PubMed] [Google Scholar]
  10. Geoffroy C., Alouf J. E. Molecular cloning and characterization of Bacillus alvei thiol-dependent cytolytic toxin expressed in Escherichia coli. J Gen Microbiol. 1988 Jul;134(7):1961–1970. doi: 10.1099/00221287-134-7-1961. [DOI] [PubMed] [Google Scholar]
  11. Geoffroy C., Alouf J. E. Selective purification by thiol-disulfide interchange chromatography of alveolysin, a sulfhydryl-activated toxin of Bacillus alvei. Toxin properties and interaction with cholesterol and liposomes. J Biol Chem. 1983 Aug 25;258(16):9968–9972. [PubMed] [Google Scholar]
  12. Geoffroy C., Gilles A. M., Alouf J. E. The sulfhydryl groups of the thiol-dependent cytolytic toxin from Bacillus alvei evidence for one essential sulfhydryl group. Biochem Biophys Res Commun. 1981 Apr 15;99(3):781–788. doi: 10.1016/0006-291x(81)91233-x. [DOI] [PubMed] [Google Scholar]
  13. Gold L., Pribnow D., Schneider T., Shinedling S., Singer B. S., Stormo G. Translational initiation in prokaryotes. Annu Rev Microbiol. 1981;35:365–403. doi: 10.1146/annurev.mi.35.100181.002053. [DOI] [PubMed] [Google Scholar]
  14. Kehoe M. A., Miller L., Walker J. A., Boulnois G. J. Nucleotide sequence of the streptolysin O (SLO) gene: structural homologies between SLO and other membrane-damaging, thiol-activated toxins. Infect Immun. 1987 Dec;55(12):3228–3232. doi: 10.1128/iai.55.12.3228-3232.1987. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Kuhn M., Kathariou S., Goebel W. Hemolysin supports survival but not entry of the intracellular bacterium Listeria monocytogenes. Infect Immun. 1988 Jan;56(1):79–82. doi: 10.1128/iai.56.1.79-82.1988. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Mengaud J., Chenevert J., Geoffroy C., Gaillard J. L., Cossart P. Identification of the structural gene encoding the SH-activated hemolysin of Listeria monocytogenes: listeriolysin O is homologous to streptolysin O and pneumolysin. Infect Immun. 1987 Dec;55(12):3225–3227. doi: 10.1128/iai.55.12.3225-3227.1987. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. Mengaud J., Vicente M. F., Chenevert J., Pereira J. M., Geoffroy C., Gicquel-Sanzey B., Baquero F., Perez-Diaz J. C., Cossart P. Expression in Escherichia coli and sequence analysis of the listeriolysin O determinant of Listeria monocytogenes. Infect Immun. 1988 Apr;56(4):766–772. doi: 10.1128/iai.56.4.766-772.1988. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. Pinkney M., Beachey E., Kehoe M. The thiol-activated toxin streptolysin O does not require a thiol group for cytolytic activity. Infect Immun. 1989 Aug;57(8):2553–2558. doi: 10.1128/iai.57.8.2553-2558.1989. [DOI] [PMC free article] [PubMed] [Google Scholar]
  19. Portnoy D. A., Jacks P. S., Hinrichs D. J. Role of hemolysin for the intracellular growth of Listeria monocytogenes. J Exp Med. 1988 Apr 1;167(4):1459–1471. doi: 10.1084/jem.167.4.1459. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. Prigent D., Alouf J. E. Interaction of steptolysin O with sterols. Biochim Biophys Acta. 1976 Aug 16;443(2):288–300. doi: 10.1016/0005-2736(76)90511-3. [DOI] [PubMed] [Google Scholar]
  21. Reboli A. C., Bryan C. S., Farrar W. E. Bacteremia and infection of a hip prosthesis caused by Bacillus alvei. J Clin Microbiol. 1989 Jun;27(6):1395–1396. doi: 10.1128/jcm.27.6.1395-1396.1989. [DOI] [PMC free article] [PubMed] [Google Scholar]
  22. Sanger F., Nicklen S., Coulson A. R. DNA sequencing with chain-terminating inhibitors. Proc Natl Acad Sci U S A. 1977 Dec;74(12):5463–5467. doi: 10.1073/pnas.74.12.5463. [DOI] [PMC free article] [PubMed] [Google Scholar]
  23. Sarvas M. Protein secretion in bacilli. Curr Top Microbiol Immunol. 1986;125:103–125. doi: 10.1007/978-3-642-71251-7_8. [DOI] [PubMed] [Google Scholar]
  24. Saunders F. K., Mitchell T. J., Walker J. A., Andrew P. W., Boulnois G. J. Pneumolysin, the thiol-activated toxin of Streptococcus pneumoniae, does not require a thiol group for in vitro activity. Infect Immun. 1989 Aug;57(8):2547–2552. doi: 10.1128/iai.57.8.2547-2552.1989. [DOI] [PMC free article] [PubMed] [Google Scholar]
  25. Thelestam M., Alouf J. E., Geoffroy C., Möllby R. Membrane-damaging action of alveolysin from Bacillus alvei. Infect Immun. 1981 Jun;32(3):1187–1192. doi: 10.1128/iai.32.3.1187-1192.1981. [DOI] [PMC free article] [PubMed] [Google Scholar]
  26. Tweten R. K. Nucleotide sequence of the gene for perfringolysin O (theta-toxin) from Clostridium perfringens: significant homology with the genes for streptolysin O and pneumolysin. Infect Immun. 1988 Dec;56(12):3235–3240. doi: 10.1128/iai.56.12.3235-3240.1988. [DOI] [PMC free article] [PubMed] [Google Scholar]
  27. Walker J. A., Allen R. L., Falmagne P., Johnson M. K., Boulnois G. J. Molecular cloning, characterization, and complete nucleotide sequence of the gene for pneumolysin, the sulfhydryl-activated toxin of Streptococcus pneumoniae. Infect Immun. 1987 May;55(5):1184–1189. doi: 10.1128/iai.55.5.1184-1189.1987. [DOI] [PMC free article] [PubMed] [Google Scholar]

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