Hemolysin

Abstract: J.E. Alouf and J.H. Freer, Preface. U. Dobrindt and J. Hacker, Plasmids, Phages, and Pathogenicity Islands: Lesson on the Evolution of Bacterial Toxins. Toxins Acting on Cytosolic Targets: P. Bouquet, The RAS Superfamily of Small GTP-Binding Proteins as Targets for Bacterial Toxins. S. Olsnes, J. Wesche, and P. . Falnes, Binding, Uptake, Routing, and Translocation of Toxins with Intracellular Sites of Action. R.K. Holmes and J.G. Siekierke, Regulation of Diptheria Toxin Production. T. Hirst, Cholera Toxin and E. Coli Heat-Labile Enterotoxins. C. Locht and R. Antoine, Bordetella Pertussis Protein Toxins. M. Thelestam, E. Chavez-Olarte, M. Moos, and C. von Eichel Streiber, Clostridial Toxins Acting on the Cytoskeleton. M.R. Popoff and J.-C. Marvaud, Structural and Genomic Features of Clostridial Neurotoxins. J. Herreros, G. Lalli, C. Montecucco, and G. Schiavo, Pathophysiological Properties of Clostridial Neurotoxins. D.W.K. Acheson and G.T. Keusch, The Family of Shiga Toxins. S.A. Leppla, The Bifactorial Bacillus Anthracis Lethal and Oedema Toxins. C. Montecucco, E. Papini, M. de Bernard, J.R. Telford, and R. Rappuoli, Helicobacter Pylori Vacuolating Cytotoxin and Associated Pathogenic Factors. Membrane-Damaging Toxins: G. Menestrina and B.V. SemjCn, Biophysical Methods and Membrane Models for the Study of Bacterial Pore Forming Cytolysins. R.W. Titball, Membrane Damaging and Cytotoxic Phospholipases. A. Ludwig and W. Goebel, The Family of the Multigenic Encoded RTX Toxins. V. Braun and R. Hertle, The Family of Serratia and Proteus Cytolsins. J.T. Buckley, The Channel-Forming Toxin Aerolysin. S. Shindoa, Vibrio Cholerae and Other Vibrio Species Haemolysins. J. Dufourcq, S. Castano, and J.-C. Talbot, Toxin, d-Related Hemolytic Toxins and Peptide Analogues. G. Prevost, Staphylococcal Bi-Component Leucotoxins. M.S. Gilmore, M. Callegan, and B. Jett, Multicomponent Cytolysins of Enterococcus Faecalis and Bacillus Cereus. R.K. Tweten and B.R. Sellman, Clostridium Septicum Pore-Forming and Lethal a-Toxin. J.E. Alouf, The Family of the Cholesterol-Binding Cytolysins. J.E. Alouf and M. Palmer, Streptolysin O (SLO). T.J. Mitchell, Pneumolysin: Structure, Function, and Role in Disease. J. Rossjohn, R.K. Tweten, J.I. Rood, and M. Parker, Perfringolysin O. T. Jacobs, A. Darji, S. Weiss, and T. Chakraborty, Listeriolysin, the Thiol-Activated Hemolysin of Listeria Monocytogenes. Other Toxins of Clinical, Pharmacologic, and Therapeutic Interest: J.D. Dubreuil, Enterotoxigenic Escherichia Coli Heat-Stable Toxins. T. Takeda, K.-I. Yoshino, T. Ramamurthy, and G.B. Nair, Heat-Stable Enterotoxins of Vibrio and Yersinia Species. C.L. Sears, Bacteroides Fragilis Toxins. J.E. Alouf, H. Muller-Alouf, and W. Koehler, Superantigenic Streptococcus Pyogenes Erythrogenic/Pyrogenic Exotoxins and Other Mitogens. S.R. Monday and G.A. Bohach, Properties of Staphylococcus Aureus Enterotoxins and Toxic Shock Syndrome Toxin-1. C. Carnoy and M. Simonet, Yersinia Pseudotuberculosis Superantigenic Toxins. D.L. Stevens and A.E. Bryant, The Pathogenesis of Shock and Tissue Injury in Clostridia Gas Gangrene. B. Koenig, A. Drynda, A. Ambrosch, and W. Koenig, Toxin-Induced Modulation of Inflammatory Processes. Y. Piimont, Staphylococcal Epidermolytic Toxins. P.E. Granum and S. Brynestad, Bacterial Toxins as Food Poisons. J.C. VanderSpek and J.R. Murphy, Diphtheria Toxins-Based Interleukin 2 Fusion Proteins. A.-M. Svennerholm and J. Holmgren, Toxin-Based Vaccines for Cholera and Escherichia Coli Diarrheas.

Abstract: Insertion of the erythromycin-resistance transposon Tn551 into the Staphylococcus aureus chromosome at a site which maps between the purB and ilv loci has a pleiotrophic effect on the production of a number of extracellular proteins. Production of alpha, beta and delta hemolysin, toxic shock syndrome toxin (TSST-1) and staphylokinase was depressed about fifty-fold while protein A production was elevated twenty-fold. Hybridization analysis showed that the defect in expression of TSST-1 and alpha hemolysin was at the transcriptional level. Inability of the mutant strain to express either a cloned TSST-1 gene or the chromosomal gene indicates that the transposon has inactivated a trans-active positive control element. This element has been designated agr for accessory gene regulator.

Abstract: Two newly discovered immune modulators, chemotaxis inhibitory protein of Staphylococcus aureus (CHIPS) and staphylococcal complement inhibitor (SCIN), cluster on the conserved 3' end of beta-hemolysin (hlb)-converting bacteriophages (betaC-phis). Since these betaC-phis also carry the genes for the immune evasion molecules staphylokinase (sak) and enterotoxin A (sea), this 8-kb region at the 3' end of betaC-phi represents an innate immune evasion cluster (IEC). By PCR and Southern analyses of 85 clinical Staphylococcus aureus strains and 5 classical laboratory strains, we show that 90% of S. aureus strains carry a betaC-phi with an IEC. Seven IEC variants were discovered, carrying different combinations of chp, sak, or sea (or sep), always in the same 5'-to-3' orientation and on the 3' end of a betaC-phi. From most IEC variants we could isolate active bacteriophages by mitomycin C treatment, of which lysogens were generated in S. aureus R5 (broad phage host). All IEC-carrying bacteriophages integrated into hlb, as was measured by Southern blotting of R5 lysogens. Large quantities of the different bacteriophages were obtained by mitomycin C treatment of the lysogens, and bacteriophages were collected and used to reinfect all lysogenic R5 strains. In total, five lytic families were found. Furthermore, phage DNA was isolated and digested with EcoR1, revealing that one IEC variant can be found on different betaI-phis. In conclusion, the four human-specific innate immune modulators SCIN, CHIPS, SAK, and SEA form an IEC that is easily transferred among S. aureus strains by a diverse group of beta-hemolysin-converting bacteriophages.