Streptococcal β-hemolysins: Genetics and role in disease pathogenesis

Trends in Microbiology

Volumn 10, Issue 12, 2002, Pages 575-580

  Nizet, Victor ^a  

^a UNIVERSITY OF CALIFORNIA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

AGAR; BACTERIAL TOXIN; CYTOLYSIN; EXOTOXIN; HEMOLYSIN; STREPTOLYSIN S; VIRULENCE FACTOR;

AGAR MEDIUM; BACTERIAL GENE; BACTERIAL GENETICS; BACTERIAL VIRULENCE; BACTERIUM COLONY; BACTERIUM MUTANT; BETA HEMOLYTIC STREPTOCOCCUS; CELL SURFACE; GENE LOCUS; HEMOLYSIS; MOLECULAR WEIGHT; MUTATIONAL ANALYSIS; NONHUMAN; PHENOTYPE; PRIORITY JOURNAL; PROTEIN DETERMINATION; PROTEIN FUNCTION; PROTEIN PURIFICATION; PROTEIN STABILITY; REVIEW; STREPTOCOCCUS AGALACTIAE; STREPTOCOCCUS GROUP A; STREPTOCOCCUS INFECTION;

BACTERIA (MICROORGANISMS); POSIBACTERIA; STREPTOCOCCUS; STREPTOCOCCUS AGALACTIAE; STREPTOCOCCUS SP. 'GROUP A'; STREPTOCOCCUS SP. 'GROUP B';

EID: 0036966408     PISSN: 0966842X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0966-842X(02)02473-3     Document Type: Article

References (60)

1. Breese B.B., Disney F.A. The accuracy of diagnosis of beta-streptococcal infection on clinical grounds. J. Pediatr. 44:1954;670-673.
2. Bisno A.L., et al. Practice guidelines for the diagnosis and management of group A streptococcal pharyngitis. Clin. Infect. Dis. 35:2002;113-125.
3. Kaufhold A., Ferrieri P. The microbiologic aspects, including diagnosis, of beta-hemolytic streptococcal and enterococcal infections. Infect. Dis. Clin. North Am. 7:1993;235-256.
4. Carey J.C. Screening and management protocols for group B streptococcus in pregnancy. Curr. Womens Health Rep. 2:2002;238-244.
5. Weld J. The toxic properties of serum extracts of hemolytic streptococci. J. Exp. Med. 59:1934;83-95.
6. Todd E.W. The differentiation of two distinct serological varieties of streptolysins: streptolysin O and streptolysin S. J. Pathol. Bacteriol. 47:1938;423-445.
7. Ginsburg I. Mechanisms of cell and tissue injury induced by group A streptococci: relation to poststreptococcal sequelae. J. Infect. Dis. 126:1972;294-340.
8. Ginsburg I., et al. Can we learn from the pathogenetic strategies of group A hemolytic streptococci how tissues are injured and organs fail in post-infectious and inflammatory sequelae? FEMS Immunol. Med. Microbiol. 25:1999;325-338.
9. Wannamaker L.W. Streptococcal toxins. Rev. Infect. Dis. 5:(Suppl. 4):1983;S723-S732.
10. Marchlewicz B.A., Duncan J.L. Properties of a hemolysin produced by group B streptococci. Infect. Immun. 30:1980;805-813.
11. Alouf J.E., Loridan C. Production, purification, and assay of streptolysin S. Methods Enzymol. 165:1988;59-64.
12. McCormick J.K., Schlievert P.M. Toxins and superantigens of group A streptococci. Fischetti V.A., et al. Gram-Positive Pathogens. 2000;43-52 ASM Press.
13. Roggiani M., et al. Exotoxins of Streptococcus pyogenes. Stevens D.L., Kaplan E.L. Streptococcal Infections: Clinical Aspects, Microbiology, and Molecular Pathogenesis. 2000;57-75 Oxford University Press.
14. Koyama J. Biochemical studies on streptolysin S II. Properties of a polypeptide component and its role in the toxin activity. J. Biochem. 54:1963;146-151.
15. Ginsburg I. Is streptolysin S of group A streptococci a virulence factor? APMIS. 107:1999;1051-1059.
16. Ofek I., et al. Inability of toxin inhibitors to neutralize enhanced toxicity caused by bacteria adherent to tissue culture cells. Infect. Immun. 58:1990;3737-3742.
17. Carr A., et al. Similarities between complement-mediated and streptolysin S-mediated hemolysis. J. Biol. Chem. 276:2001;41790-41796.
18. Bernheimer A.W. Physical behavior of streptolysin S. J. Bacteriol. 93:1967;2024-2025.
19. Wannamaker L.W., Schlievert P.M. Exotoxins of the group A streptococci. Hardegree M.C., Tu A.T. Handbook of Natural Toxins, Vol. 4, Bacterial Toxins. 1988;267-295 Marcel Dekker.
20. Weller U., et al. Expression of active streptolysin O in Escherichia coli as a maltose-binding-protein-streptolysin-O fusion protein. The N-terminal 70 amino acids are not required for hemolytic activity. Eur. J. Biochem. 236:1996;34-39.
21. Palmer M. The family of thiol-activated, cholesterol-binding cytolysins. Toxicon. 39:2001;1681-1689.
22. Borgia S.M., et al. Cloning of a chromosomal region responsible for streptolysin S production in Streptococcus pyogenes. Adv. Exp. Med. Biol. 418:1997;733-736.
23. Nizet V., et al. Genetic locus for streptolysin S production by group A Streptococcus. Infect. Immun. 68:2000;4245-4254.
24. Ferretti J.J., et al. Complete genome sequence of an M1 strain of Streptococcus pyogenes. Proc. Natl. Acad. Sci. U. S. A. 98:2001;4658-4663.
25. Jack R.W., et al. Bacteriocins of Gram-positive bacteria. Microbiol. Rev. 59:1995;171-200.
26. Sahl H.G., Bierbaum G. Lantibiotics: biosynthesis and biological activities of uniquely modified peptides from Gram-positive bacteria. Annu. Rev. Microbiol. 52:1998;41-79.
27. Dale J.B., et al. Antibodies against a synthetic peptide of SagA neutralize the cytolytic activity of streptolysin S from group A streptococci. Infect. Immun. 70:2002;2166-2170.
28. Kihlberg B.M., et al. Biological properties of a Streptococcus pyogenes mutant generated by Tn916 insertion in mga. Microb. Pathog. 19:1995;299-315.
29. Federle M.J., et al. A response regulator that represses transcription of several virulence operons in the group A Streptococcus. J. Bacteriol. 181:1999;3649-3657.
30. Heath A., et al. A two-component regulatory system, CsrR-CsrS, represses expression of three Streptococcus pyogenes virulence factors, hyaluronic acid capsule, streptolysin S, and pyrogenic exotoxin B. Infect. Immun. 67:1999;5298-5305.
31. Beckert S., et al. Group A streptococcal rofA gene is involved in the control of several virulence genes and eukaryotic cell attachment and internalization. Infect. Immun. 69:2001;534-537.
32. Kreikemeyer B., et al. Group A streptococcal growth phase-associated virulence factor regulation by a novel operon (Fas) with homologies to two-component-type regulators requires a small RNA molecule. Mol. Microbiol. 39:2001;392-406.
33. Li Z., et al. Identification of pel, a Streptococcus pyogenes locus that affects both surface and secreted proteins. J. Bacteriol. 181:1999;6019-6027.
34. Eberhard T.H., et al. Mouse skin passage of a Streptococcus pyogenes Tn917 mutant of sagA/pel restores virulence, beta-hemolysis and sagA/pel expression without altering the position or sequence of the transposon. BMC Microbiol. 1:2001;33.
35. Biswas I., et al. Generation and surface localization of intact M protein in Streptococcus pyogenes are dependent on sagA. Infect. Immun. 69:2001;7029-7038.
36. Humar D., et al. Streptolysin S and necrotising infections produced by group G Streptococcus. Lancet. 359:2002;124-129.
37. Fuller, J.D. et al. Discovery of a streptolysin S-associated gene cluster and its role in the pathogenesis of Streptococcus iniae disease. Infect. Immun. (in press).
38. Betschel S.D., et al. Reduced virulence of group A streptococcal Tn916 mutants that do not produce streptolysin S. Infect. Immun. 66:1998;1671-1679.
39. Limbago B., et al. Role of streptolysin O in a mouse model of invasive group A streptococcal disease. Infect. Immun. 68:2000;6384-6390.
40. Ginsburg I. Could synergistic interactions among reactive oxygen species, proteinases, membrane-perforating enzymes, hydrolases, microbial hemolysins and cytokines be the main cause of tissue damage in infectious and inflammatory conditions? Med. Hypotheses. 51:1998;337-346.
41. Spellerberg B. Pathogenesis of neonatal Streptococcus agalactiae infections. Microbes Infect. 2:2000;1733-1742.
42. Nizet V., Rubens C.E. Pathogenic mechanisms and virulence factors of group B streptococci. Fischetti V.A., et al. The Gram-Positive Pathogens. 2000;125-136 ASM Press.
43. Pritzlaff C.A., et al. Genetic basis for the beta-haemolytic/cytolytic activity of group B Streptococcus. Mol. Microbiol. 39:2001;236-247.
44. Tapsall J.W. Relationship between pigment production and haemolysin formation by Lancefield group B streptococci. J. Med. Microbiol. 24:1987;83-87.
45. Spellerberg B., et al. The cyl genes of Streptococcus agalactiae are involved in the production of pigment. FEMS Microbiol. Lett. 188:2000;125-128.
46. Nizet V., et al. Group B streptococcal beta-hemolysin expression is associated with injury of lung epithelial cells. Infect. Immun. 64:1996;3818-3826.
47. Gibson R.L., et al. Group B streptococcal beta-hemolysin promotes injury of lung microvascular endothelial cells. Pediatr. Res. 45:1999;626-634.
48. Nizet V., et al. Invasion of brain microvascular endothelial cells by group B streptococci. Infect. Immun. 65:1997;5074-5081.
49. Ring A., et al. Group B streptococcal beta-hemolysin induces nitric oxide production in murine macrophages. J. Infect. Dis. 182:2000;150-157.
50. Henneke P., et al. Cellular activation, phagocytosis, and bactericidal activity against Group B Streptococcus involve separate but parallel MyD88 dependent and MyD88 independent signaling pathways. J. Immunol. 169:2002;3970-3977.
51. Doran K.S., et al. Group B streptococcal beta-hemolysin/cytolysin promotes invasion of human lung epithelial cells and the release of interleukin-8. J. Infect. Dis. 185:2002;196-203.
52. Nizet V., et al. The role of group B streptococci beta-hemolysin expression in newborn lung injury. Adv. Exp. Med. Biol. 418:1997;627-630.
53. Puliti M., et al. Severity of group B streptococcal arthritis is correlated with beta-hemolysin expression. J. Infect. Dis. 182:2000;824-832.
54. Ring A., et al. Group B streptococcal beta-hemolysin induces mortality and liver injury in experimental sepsis. J. Infect. Dis. 185:2002;1745-1753.
55. Tapsall J.W., Phillips E.A. The hemolytic and cytolytic activity of group B streptococcal hemolysin and its possible role in early onset group B streptococcal disease. Pathology. 23:1991;139-144.
56. Talati A.J., et al. Immunomodulation by exogenous surfactant: effect on TNF-alpha secretion and luminol-enhanced chemiluminescence activity by murine macrophages stimulated with group B streptococci. Microbes Infect. 3:2001;267-273.
57. Fettucciari K., et al. Group B Streptococcus induces apoptosis in macrophages. J. Immunol. 165:2000;3923-3933.
58. Nizet V., et al. Molecular pathogenesis of group B streptococcal disease in newborns. Stevens D.L., Kaplan E.L. Streptococcal Infections: Clinical Aspects, Microbiology, and Molecular Pathogenesis. 2000;180-221 Oxford University Press.
59. Herting E., et al. Surfactant improves lung function and mitigates bacterial growth in immature ventilated rabbits with experimentally induced neonatal group B streptococcal pneumonia. Arch. Dis. Child. Fetal Neonatal Ed. 76:1997;F3-8.
60. Herting E., et al. Surfactant treatment of neonates with respiratory failure and group B streptococcal infection. Members of the Collaborative European Multicenter Study Group. Pediatrics. 106:2000;957-964.