1887

Abstract

Summary

Twelve diverse strains of of clinical origin all produced a calcium-dependent haemolysin, unlike most other spp. In most strains the haemolysin was secreted into the medium during early exponential growth and lysed not only of a variety of erythrocyte types from several animals including man, but also human neutrophils and human embryo lung fibroblasts. The haemolysin was a protein of 107 kDa, the same size as H1yA, and it reacted with antiserum to H1yA. Because of its similarity in size, antigenicity and range of action to the H1yA virulence factor of H1yA is believed to be an important virulence factor for this organism. It was degradable by an EDTA-sensitive protease—probably the IgA protease—to inactive fragments. The interaction of H1yA and IgA protease and the origin of H1yA, which has now been found in many diverse bacteria, are discussed.

Loading

Article metrics loading...

/content/journal/jmm/10.1099/00222615-39-4-282
1993-10-01
2022-05-16
Loading full text...

Full text loading...

/deliver/fulltext/jmm/39/4/medmicro-39-4-282.html?itemId=/content/journal/jmm/10.1099/00222615-39-4-282&mimeType=html&fmt=ahah

References

  1. Bhakdi S, Greulich S, Muhly M et al. Potent leukocidal action of Escherichia coli hemolysin mediated by permeabilization of target cell membranes. J Exp Med 1989; 169:737–754
    [Google Scholar]
  2. Kamp EM, van Leengoed LAMG. Serotype-related differences in production and type of heat-labile hemolysin and heat-labile cytotoxin of Actinobacillus (Haemophilus) pleuro-pneumoniae. J Clin Microbiol 1989; 27:1187–1191
    [Google Scholar]
  3. Glaser P, Sakamoto H, Bellalou J, Ullmann A, Danchin A. Secretion of cyclolysin, the calmodulin-sensitive adenylate cyclase-haemolysin bifunctional protein of Bordetella pertussis. EM BO J 1988; 7:3997–4004
    [Google Scholar]
  4. Shewen PE, Wilkie BN. Cytotoxin of Pasteurella haemolytica acting on bovine leukocytes. Infect Immun 1982; 35:91–94
    [Google Scholar]
  5. Tsai C-C, Shenker BJ, Dirienzo JM, Malamud D, Taiehman NS. Extraction and isolation of leukotoxin from Actinobacillus actinomycetemcomitans with polymyxin B. Infect Immun 1984; 43:700–705
    [Google Scholar]
  6. Welch RA. Pore-forming cytolysins of Gram-negative bacteria. Mol Microbiol 1991; 5:521–528
    [Google Scholar]
  7. Cavalieri SJ, Snyder IS. Effect of Escherichia coli alpha-hemolysin on human peripheral leukocyte function in vitro. Infect Immun 1982; 37:966–974
    [Google Scholar]
  8. Hickman FW, Steigerwalt AG, Farmer JJ, Brenner DJ. Identification of Proteus penneri sp. nov., formerly known as Proteus vulgaris indole negative or as Proteus vulgaris biogroup 1. J Clin Microbiol 1982; 15:1097–1102
    [Google Scholar]
  9. Krajden S, Fuksa M, Lizewski W, Barton L, Lee A. Proteus penneri and urinary calculi formation. J Clin Microbiol 1984; 19:541–542
    [Google Scholar]
  10. Krajden S, Fuksa M, Petrea C, Crisp LJ, Penner JL. Expanded clinical spectrum of infections caused by Proteus penneri. J Clin Microbiol 1987; 25:578–579
    [Google Scholar]
  11. Muller HE. Occurrence and pathogenic role of Morganella-Proteus-Providencia group bacteria in human feces. J Clin Microbiol 1986; 23:404–405
    [Google Scholar]
  12. Mobley HLT, Jones BD, Penner JL. Urease activity of Proteus penneri. J Clin Microbiol 1987; 25:2302–2305
    [Google Scholar]
  13. Senior BW, Albrechtsen M, Kerr MA. A survey of IgA protease production among clinical isolates of Proteeae. J Med Microbiol 1988; 25:27–31
    [Google Scholar]
  14. Loomes LM, Senior BW, Kerr MA. Proteinases of Proteus spp.: purification, properties, and detection in urine of infected patients. Infect Immun 1992; 60:2267–2273
    [Google Scholar]
  15. Yakubu DE, Old DC, Senior BW. The haemagglutinins and fimbriae of Proteus penneri. J Med Microbiol 1989; 30:279–284
    [Google Scholar]
  16. Knapp S, Hacker J, Then I, Muller D, Goebel W. Multiple copies of hemolysin genes and associated sequences in the chromosome of uropathogenic Escherichia coli strains. J Bacteriol 1984; 159:1027–1033
    [Google Scholar]
  17. Koronakis V, Cross M, Senior B, Koronakis E, Hughes C. The secreted hemolysins of Proteus mirabilis, Proteus vulgaris, and Morganella morganii are genetically related to each other and to the alpha-hemolysin of Escherichia coli. J Bacteriol 1987; 169:1509–1515
    [Google Scholar]
  18. Senior BW, Hughes C. Production and properties of haem-olysins from clinical isolates of the Proteeae. J Med Microbiol 1988; 25:17–25
    [Google Scholar]
  19. Swihart KG, Welch RA. The HpmA hemolysin is more common than HlyA among Proteus isolates. Infect Immun 1990; 58:1853–1860
    [Google Scholar]
  20. Senior BW, Leslie DL. Rare occurrence of Proteus vulgaris in faeces: a reason for its rare association with urinary tract infections. J Med Microbiol 1986; 21:139–144
    [Google Scholar]
  21. Swihart KG, Welch RA. Cytotoxic activity of the Proteus hemolysin HpmA. Infect Immun 1990; 58:1861–1869
    [Google Scholar]
  22. Mobley HLT, Chippendale GR, Swihart KG, Welch RA. Cytotoxicity of the HpmA hemolysin and urease of Proteus mirabilis and Proteus vulgaris against cultured renal proximal tubular epithelial cells. Infect Immun 1991; 59:2036–2042
    [Google Scholar]
  23. Eberspacher B, Hugo F, Pohl M, Bhakdi S. Functional similarity between the haemolysins of Escherichia coli and Morganella morganii. J Med Microbiol 1990; 33:165–170
    [Google Scholar]
  24. Emody L, Voros S, Pal T. Alpha-haemolysin, a possible virulence factor in Proteus morganii. FEMS Microbiol Lett 1982; 13:329–331
    [Google Scholar]
  25. Voros S, Senior BW. New O antigens of Morganella morganii and the relationships between haemolysin production, O antigens and morganocin types of strains. Acta Microbiol Hung 1990; 37:341–349
    [Google Scholar]
  26. Wandersman C, Delepelaire P. Tol C, an Escherichia coli outer membrane protein required for hemolysin secretion. Proc Natl Acad Sci USA 1990; 87:4776–4780
    [Google Scholar]
  27. Koronakis V, Stanley P, Koronakis E, Hughes C. The HlyB/HlyD-dependent secretion of toxins by Gram-negative bacteria. FEMS Microbiol Immunol 1992; 105:45–54
    [Google Scholar]
  28. Ostolaza H, Bartoleme B, Serra JL, de la Cruz F, Goni FM. α-Hemolysin from E. coli: purification and self-aggregation properties. FEBS Lett 1991; 280:195–198
    [Google Scholar]
  29. Felmlee T, Pellett S, Welch RA. Nucleotide sequence of an Escherichia coli chromosomal hemolysin. J Bacteriol 1985; 163:94–105
    [Google Scholar]
http://instance.metastore.ingenta.com/content/journal/jmm/10.1099/00222615-39-4-282
Loading
/content/journal/jmm/10.1099/00222615-39-4-282
Loading

Data & Media loading...

This is a required field
Please enter a valid email address
Approval was a Success
Invalid data
An Error Occurred
Approval was partially successful, following selected items could not be processed due to error