Reduced Virulence of Group A Streptococcal Tn916 Mutants That Do Not Produce Streptolysin S

Infection and Immunity

Volumn 66, Issue 4, 1998, Pages 1671-1679

  Betschel, Stephen D ^a   Borgia, Sergio M ^a   Barg, Neil L ^b   Low, Donald E ^a   De Azavedo, Joyce C S ^a  

^a MOUNT SINAI HOSPITAL   (Canada)

^b UNIVERSITY OF MICHIGAN MEDICAL SCHOOL   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; STREPTOLYSIN; STREPTOLYSIN S;

AMINO ACID SEQUENCE; ANIMAL; ARTICLE; BACTERIUM CONJUGATION; HEMOLYSIS; MOLECULAR GENETICS; MOUSE; MUTATION; NUCLEOTIDE SEQUENCE; PATHOGENICITY; PATHOLOGY; STREPTOCOCCUS INFECTION; STREPTOCOCCUS PYOGENES; TRANSPOSON; VIRULENCE;

AMINO ACID SEQUENCE; ANIMALS; BACTERIAL PROTEINS; BASE SEQUENCE; CONJUGATION, GENETIC; DNA TRANSPOSABLE ELEMENTS; HEMOLYSIS; MICE; MOLECULAR SEQUENCE DATA; MUTATION; STREPTOCOCCAL INFECTIONS; STREPTOCOCCUS PYOGENES; STREPTOLYSINS; VIRULENCE;

EID: 0032036480     PISSN: 00199567     EISSN: None     Source Type: Journal    
DOI: 10.1128/iai.66.4.1671-1679.1998     Document Type: Article

References (36)

1. Akao, T., T. Takahashi, and K. Kobashi. 1992. Purification and characterization of a peptide essential for formation of streptolysin S by Streptococcus pyogenes. Infect. Immun. 60:4777-4780.
2. Alouf, J. E. 1980. Streptococcal toxins (streptolysin O, streptolysin S, erythrogenic toxin). Pharmacol. Ther. 11:661-717.
3. Barnard, W. G., and E. W. Todd. 1940. Lesions in mouse produced by streptolysins O and S. J. Pathol. Bacteriol. 51:43-47.
4. Bernheimer, A. W. 1954. Streptococcal infections, p. 19. Columbia University Press, New York, N.Y.
5. Bernheimer, A. W. 1972. Hemolysins of streptococci: characterization and effects on biological membranes, p. 19-31. In L. W. Wannamaker and J. M. Matson (ed.), Streptococci and streptococcal diseases. Academic Press, New York, N.Y.
6. Bunce, C., L. Wheeler, G. Reed, J. Musser, and N. Barg. 1992. A murine model of cutaneous infection with gram-positive cocci. Infect. Immun. 60: 2636-2640.
7. Clewell, D. B., and S. E. Flannagan. 1993. The conjugative transposons of gram-positive bacteria, p. 369-393. Plenum Press, New York, N.Y.
8. Dougherty, B. A., and I. Van de Rijn. 1992. Molecular characterization of a locus required for hyaluronic acid capsule production in group A streptococci. J. Exp. Med. 175:1291-1299.
9. Fischetti, V. A., K. F. Jones, and J. R. Scott. 1985. Size variation of the M protein in group A streptococci. J. Exp. Med. 161:1384-1401.
10. Freer, J. H., and J. P. Arbuthnott. 1976. Biochemical and morphological alterations of membranes by bacterial toxins, p. 170-193. In A. W. Bernheimer (ed.). Mechanisms in bacterial toxinology. John Wiley and Sons, New York, N.Y.
11. Gawron-Burke, C., and D. B. Clewell. 1982. A transposon in Streptococcus faecalis with fertility properties. Nature (London) 300:281-284.
12. Gawron-Burke, C., and D. B. Clewell. 1984. Regeneration of insertionally inactivated streptococcal DNA fragments after excision of transposon Tn916 in Escherichia coli: strategy for targeting and cloning of genes from gram-positive bacteria. J. Bacteriol. 159:214-221.
13. Gilman, M. 1997. Preparation of RNA from eukaryotic and prokaryotic cells, p. 4.1.1-4.1.23. In F. M. Ausubel, R. Brent, R. E. Kingston, D. D. Moore, J. G. Seidman, J. A. Smith, and K. Struhl (ed.), Current protocols in molecular biology. John Wiley and Sons, New York, N.Y.
14. Ginsburg, I. 1970. Streptolysin S. p. 99-171. In T. C. Montie, S. Kadis, and S. J. Ajl (ed.), Microbial toxins. Academic Press, New York, N.Y.
15. Ginsburg, I., Z. Bentwich, N. Zeiri, Z. Silberstein, and S. Lav. 1968. Mechanism of action of streptolysin S, p. 239-254. In R. Caravano (ed.), Current research on group A streptococci. Excerpta Medical Foundation, Amsterdam, The Netherlands.
16. Griffith, F. 1934. Serological classification of Streptococcus pyogenes. J. Hyg. (London) 34:542-584.
17. Hare, R. 1937. Heat-labile toxin of hemolytic streptococci. J. Pathol. Bacteriol. 44:71-90.
18. Jelijaszwicz, J., S. Szmigielski, and W. Hryniewicz. 1978. Biological effects of staphylococcal and streptococcal toxins, p. 185-227. In J. S. Jelijaszewicz and T. Wadstrom (ed.), Bacterial toxins and cell membranes. Academic Press, New York, N.Y.
19. Ji, Y., L. McLandsborough, A. Kondagunta, and P. P. Cleary. 1996. C5a peptidase alters clearance and trafficking of group A streptococci by infected mice. Infect. Immun. 64:503-510.
20. Kinsman, O. S., and J. P. Arbuthnott. 1980. Experimental staphylococcal infections in newborn mice: inhibition of weight gain as an index of virulence. J. Med. Microbiol. 13:281-290.
21. Knutson, C. A., and A. Jeanes. 1968. A new modification of the carbazole analysis: application to heteropolysaccharides. Ann. Biochem. 24:470-481.
22. Koyama, J., and F. Egami. 1963. Biochemical studies on streptolysin S formed in the presence of yeast ribonucleic acid. I. The purification and some properties of the toxin. J. Biochem. (Japan) 53:147-154.
23. Laemmli, U. K. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227:680-685.
24. Lai, C. Y., M. T. Wang, J. B. De Faria, and T. Akao. 1978. Streptolysin S: improved purification and characterization. Arch. Biochem. Biophys. 191: 804-812.
25. Lu, F., and G. Churchwood. 1995. Tn916 target DNA sequences bind the C-terminal domain of integrase protein with different affinities that correlate with transposon insertion frequency. J. Bacteriol. 177:1938-1946.
26. Musser, J., S. Kanjilal, U. Shah, D. Musher, N. Barg, K. Nelson, R. K. Selander, K. Johnson, P. Schlievert, J. Henrichsen, D. Gerlach, R. Rakita, A. Tanna, B. Cookson, and J. Huang. 1993. Geographic and temporal distribution and molecular characterization of two highly pathogenic clones of Streptococcus pyogenes expressing allelic variants of pyrogenic exotoxin A (scarlet fever toxin). J. Infect. Dis. 167:337-346.
27. Nida, K., and P. P. Cleary. 1983. Insertional inactivation of streptolysin S expression in Streptococcus pyogenes. J. Bacteriol. 155:1156-1161.
28. O'Connor, S. P., and P. P. Cleary. 1987. In vivo Streptococcus pyogenes C5a peptidase activity: analysis using transposon and nitrosoguanidine-induced mutants. J. Infect. Dis. 156:495-504.
29. Owens, W., F. Henley, and B. D. Baridge. 1978. Hemolytic mutants of group A Streptococcus pyogenes. J. Clin. Microbiol. 7:153-157.
30. Pang, K. M., and D. A. Knecht. 1997. Partial inverse PCR: a technique for cloning flanking sequences. BioTechniques 22:1046-1048.
31. Sambrook, J., E. F. Fritsch, and T. Maniatis. 1989. Molecular cloning: a laboratory manual, 2nd ed., p. 1.21-1.31. Cold Spring Harbor Laboratory, Cold Spring Harbor, N.Y.
32. Schlievert, P. M., K. M. Bettin, and D. W. Watson. 1977. Purification and characterization of group A streptococcal pyrogenic exotoxin type C. Infect. Immun. 16:673-679.
33. Smyth, C. J., and J. L. Duncan. 1978. Thiol-activated (oxygen-labile) cytolysins, p. 129-183. In J. S. Jelijaszewicz and T. Wadstrom (ed.), Bacterial toxins and cell membranes. Academic Press, New York, N.Y.
34. Weld, J. T. 1934. Toxic properties of serum extracts of hemolytic streptococci. J. Exp. Med. 59:83-95.
35. Wheeler, M. C., M. H. Roe, E. L. Kaplan, P. M. Schlievert, and J. K. Todd. 1991. Outbreak of group A streptococcus septicemia in children. JAMA 266:533-537.
36. Wilson, K. 1994. Preparation of genomic DNA from bacteria, p. 2.4.1-2.4.5. In F. M. Ausubel, R. Brent, R. E. Kingston, D. D. Moore, J. G. Seidman, J. A. Smith, and K. Struhl (ed.), Current protocols in molecular biology. John Wiley and Sons, New York, N.Y.