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. 1996 Jun;64(6):2356–2358. doi: 10.1128/iai.64.6.2356-2358.1996

Neutralizing monoclonal antibodies against listeriolysin: mapping of epitopes involved in pore formation.

A Darji 1, K Niebuhr 1, M Hense 1, J Wehland 1, T Chakraborty 1, S Weiss 1
PMCID: PMC174080  PMID: 8675351

Abstract

Six different mouse monoclonal antibodies (MAbs) and a specific rabbit polygonal antibody were raised against listeriolysin. Four of the MAbs also recognized seeligeriolysin, and five cross-reacted with ivanolysin. The hemolytic activity could be neutralized by the polygonal antibody as well as by five of the MAbs. None of the neutralizing antibodies interfered with the binding of listeriolysin to the cellular membrane. The epitopes recognized by the MAbs were localized by using overlapping synthetic peptides between positions 59 and 279, a region hitherto not implicated in mediating hemolytic activity.

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Selected References

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  1. Andersen B. R., Van Epps D. E. Suppression of chemotatic activity of human neutrophils by streptolysin O. J Infect Dis. 1972 Apr;125(4):353–359. doi: 10.1093/infdis/125.4.353. [DOI] [PubMed] [Google Scholar]
  2. Arnold R., Scheffer J., König B., König W. Effects of Listeria monocytogenes and Yersinia enterocolitica on cytokine gene expression and release from human polymorphonuclear granulocytes and epithelial (HEp-2) cells. Infect Immun. 1993 Jun;61(6):2545–2552. doi: 10.1128/iai.61.6.2545-2552.1993. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. 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]
  4. Darji A., Chakraborty T., Niebuhr K., Tsonis N., Wehland J., Weiss S. Hyperexpression of listeriolysin in the nonpathogenic species Listeria innocua and high yield purification. J Biotechnol. 1995 Dec 15;43(3):205–212. doi: 10.1016/0168-1656(95)00138-7. [DOI] [PubMed] [Google Scholar]
  5. Domann E., Wehland J., Niebuhr K., Haffner C., Leimeister-Wächter M., Chakraborty T. Detection of a prfA-independent promoter responsible for listeriolysin gene expression in mutant Listeria monocytogenes strains lacking the PrfA regulator. Infect Immun. 1993 Jul;61(7):3073–3075. doi: 10.1128/iai.61.7.3073-3075.1993. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Geoffroy C., Mengaud J., Alouf J. E., Cossart P. Alveolysin, the thiol-activated toxin of Bacillus alvei, is homologous to listeriolysin O, perfringolysin O, pneumolysin, and streptolysin O and contains a single cysteine. J Bacteriol. 1990 Dec;172(12):7301–7305. doi: 10.1128/jb.172.12.7301-7305.1990. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. 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]
  8. Leimeister-Wächter M., Chakraborty T. Detection of listeriolysin, the thiol-dependent hemolysin in Listeria monocytogenes, Listeria ivanovii, and Listeria seeligeri. Infect Immun. 1989 Aug;57(8):2350–2357. doi: 10.1128/iai.57.8.2350-2357.1989. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. 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]
  10. Nato F., Reich K., Lhopital S., Rouyre S., Geoffroy C., Mazie J. C., Cossart P. Production and characterization of neutralizing and nonneutralizing monoclonal antibodies against listeriolysin O. Infect Immun. 1991 Dec;59(12):4641–4646. doi: 10.1128/iai.59.12.4641-4646.1991. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Owen R. H., Boulnois G. J., Andrew P. W., Mitchell T. J. A role in cell-binding for the C-terminus of pneumolysin, the thiol-activated toxin of Streptococcus pneumoniae. FEMS Microbiol Lett. 1994 Aug 15;121(2):217–221. doi: 10.1111/j.1574-6968.1994.tb07101.x. [DOI] [PubMed] [Google Scholar]
  12. Paton J. C., Ferrante A. Inhibition of human polymorphonuclear leukocyte respiratory burst, bactericidal activity, and migration by pneumolysin. Infect Immun. 1983 Sep;41(3):1212–1216. doi: 10.1128/iai.41.3.1212-1216.1983. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. 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]
  14. 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]
  15. Shastri N., Malissen B., Hood L. Ia-transfected L-cell fibroblasts present a lysozyme peptide but not the native protein to lysozyme-specific T cells. Proc Natl Acad Sci U S A. 1985 Sep;82(17):5885–5889. doi: 10.1073/pnas.82.17.5885. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Sibelius U., Rose F., Chakraborty T., Darji A., Wehland J., Weiss S., Seeger W., Grimminger F. Listeriolysin is a potent inducer of the phosphatidylinositol response and lipid mediator generation in human endothelial cells. Infect Immun. 1996 Feb;64(2):674–676. doi: 10.1128/iai.64.2.674-676.1996. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. Tang P., Rosenshine I., Finlay B. B. Listeria monocytogenes, an invasive bacterium, stimulates MAP kinase upon attachment to epithelial cells. Mol Biol Cell. 1994 Apr;5(4):455–464. doi: 10.1091/mbc.5.4.455. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. Tweten R. K., Harris R. W., Sims P. J. Isolation of a tryptic fragment from Clostridium perfringens theta-toxin that contains sites for membrane binding and self-aggregation. J Biol Chem. 1991 Jul 5;266(19):12449–12454. [PubMed] [Google Scholar]
  19. 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]
  20. 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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