Contribution of the ATP-dependent protease ClpCP to the autolysis and virulence of Streptococcus pneumoniae

Infection and Immunity

Volumn 73, Issue 2, 2005, Pages 730-740

  Ibrahim, Yasser Musa ^a   Kerr, Alison R ^a   Silva, Nuno A ^a   Mitchell, Tim J ^a  

^a UNIVERSITY OF GLASGOW   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATE; ADENOSINE TRIPHOSPHATE DEPENDENT CASEINOLYTIC PROTEINASE; AUTOLYSIN; AUTOLYSIN A; PNEUMOLYSIN; PROTEINASE; UNCLASSIFIED DRUG;

ADOLESCENT; ANIMAL MODEL; ANIMAL TISSUE; ARTICLE; AUTOLYSIS; BACTERIAL GROWTH; BACTERIAL STRAIN; BACTERIAL VIRULENCE; BACTERIOLYSIS; BLOOD; CONTROLLED STUDY; FEMALE; HEAT TOLERANCE; HIGH TEMPERATURE; LUNG INFECTION; MOUSE; NONHUMAN; OXIDATIVE STRESS; PRIORITY JOURNAL; PROTEIN SECRETION; SEROTYPE; STREPTOCOCCUS INFECTION; STREPTOCOCCUS PNEUMONIAE; STREPTOCOCCUS PNEUMONIAE D39;

ADENOSINE TRIPHOSPHATE; ANIMALS; BACTERIAL PROTEINS; BACTERIOLYSIS; BLOOD; DISEASE MODELS, ANIMAL; ENDOPEPTIDASE CLP; HEAT; LUNG; MICE; N-ACETYLMURAMOYL-L-ALANINE AMIDASE; OXIDATIVE STRESS; PNEUMONIA, PNEUMOCOCCAL; STREPTOCOCCUS PNEUMONIAE; STREPTOLYSINS; VIRULENCE;

EID: 12844281219     PISSN: 00199567     EISSN: None     Source Type: Journal    
DOI: 10.1128/IAI.73.2.730-740.2005     Document Type: Article

References (41)

1. Avery, O. T., C. M. Macleod, and M. McCarty. 1944. Studies on the chemical nature of the substance inducing transformation of pneumococcal types: induction of transformation by desoxyribonucleic acid fraction isolated from pneumococcus type III. J. Exp. Med. 79:137-158.
2. Balachandran, P., S. K. Hollingshead, J. C. Paton, and D. E. Briles. 2001. The autolytic enzyme LytA of Streptococcus pneumoniae is not responsible for releasing pneumolysin. J. Bacteriol. 183:3108-3116.
3. Blue, C. E., and T. J. Mitchell. 2003. Contribution of a response regulator to the virulence of Streptococcus pneumoniae is strain dependent. Infect. Immun. 71:4405-4413.
4. Bradford, M. M. 1976. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72:248-254.
5. Briese, T., and R. Hakenbeck. 1985. Interaction of the pneumococcal amidase with lipotechoic acid and choline. Eur. J. Biochem. 146:417-427.
6. Charpentier, E., R. Novak, and E. Tuomanen. 2000. Regulation of growth inhibition at high temperature, autolysis, transformation and adherence in Streptococcus pneumoniae by clpC. Mol. Microbiol. 37:717-726.
7. Chastanet, A., M. Prudhomme, J. P. Claverys, and T. Msadek. 2001. Regulation of Streptococcus pneumoniae clp genes and their role in competence development and stress survival. J. Bacteriol. 183:7295-7307.
8. Craig, E. A., B. D. Gambill, and R. J. Nelson. 1993. Heat shock proteins: molecular chaperones of protein biogenesis. Microbiol. Rev. 57:402-414.
9. Derre, I., G. Rapoport, and T. Msadek. 1999. CtsR, a novel regulator of stress and heat shock response, controls clp and molecular chaperone gene expression in gram-positive bacteria. Mol. Microbiol. 31:117-131.
10. Diaz-Torres, M. L., and R. R. Russell. 2001. HtrA protease and processing of extracellular proteins of Streptococcus mutans. FEMS Microbiol Lett. 204:23-28.
11. Frees, D., and H. Ingmer. 1999. ClpP participates in the degradation of misfolded protein in Lactococcus lactis. Mol. Microbiol. 31:79-87.
12. Gerth, U., E. Kruger, I. Derre, T. Msadek, and M. Hecker. 1998. Stress induction of the Bacillus subtilis clpP gene encoding a homologue of the proteolytic component of the Clp protease and the involvement of ClpP and ClpX in stress tolerance. Mol. Microbiol. 28:787-802.
13. Gottesman, S. 1999. Regulation by proteolysis: developmental switches. Curr. Opin. Microbiol. 2:142-147.
14. Hendrick, J. P., and F. U. Hartl. 1993. Molecular chaperone functions of heat-shock proteins. Annu. Rev. Biochem. 62:349-384.
15. Hoskins, J., W. E. Alborn, Jr., J. Arnold, L. C. Blaszczak, S. Burgett, B. S. DeHoff, S. T. Estrem, L. Fritz, D. J. Fu, W. Fuller, C. Geringer, R. Gilmour, J. S. Glass, H. Khoja, A. R. Kraft, R. E. Lagace, D. J. LeBlanc, L. N. Lee, E. J. Lefkowitz, J. Lu, P. Matsushima, S. M. McAhren, M. McHenney, K. McLeaster, C. W. Mundy, T. I. Nicas, F. H. Norris, M. O'Gara, R. B. Peery, G. T. Robertson, P. Rockey, P. M. Sun, M. E. Winkler, Y. Yang, M. Young-Bellido, G. Zhao, C. A. Zook, R. H. Baltz, S. R. Jaskunas, P. R. Rosteck, Jr., P. L. Skatrud, and J. I. Glass. 2001. Genome of the bacterium Streptococcus pneumoniae strain R6. J. Bacteriol. 183:5709-5717.
16. Johnson, S. R., B. M. Steiner, D. D. Cruce, G. H. Perkins, and R. J. Arko. 1993. Characterization of a catalase-deficient strain of Neisseria gonorrhoeae: evidence for the significance of catalase in the biology of N. gonorrhoeae. Infect. Immun. 61:1232-1238.
17. Kadioglu, A., N. A. Gingles, K. Grattan, A. Kerr, T. J. Mitchell, and P. W. Andrew. 2000. Host cellular immune response to pneumococcal lung infection in mice. Infect. Immun. 68:492-501.
18. Kerr, A. R., J. J. Irvine, J. J. Search, N. A. Gingles, A. Kadioglu, P. W. Andrew, W. L. McPheat, C. G. Booth, and T. J. Mitchell. 2002. Role of inflammatory mediators in resistance and susceptibility to pneumococcal infection. Infect. Immun. 70:1547-1557.
19. Kruger, E., U. Volker, and M. Hecker. 1994. Stress induction of clpC in Bacillus subtilis and its involvement in stress tolerance. J. Bacteriol. 176:3360-3367.
20. Kruger, E., E. Witt, S. Ohlmeier, R. Hanschke, and M. Hecker. 2000. The clp proteases of Bacillus subtilis are directly involved in degradation of misfolded proteins. J. Bacteriol. 182:3259-3265.
21. Kwon, H. Y., S. W. Kim, M. H. Choi, A. D. Ogunniyi, J. C. Paton, S. H. Park, S. N. Pyo, and D. K. Rhee. 2003. Effect of heat shock and mutations in ClpL and ClpP on virulence gene expression in Streptococcus pneumoniae. Infect. Immun. 71:3757-3765.
22. Lacks, S., and R. D. Hotchkiss. 1960. A study of the genetic material determining an enzyme activity in the pneumococcus. Biochim. Biophys. Acta 39:508-517.
23. Lefevre, J. C., J. P. Claverys, and A. M. Sicard. 1979. Donor deoxyribonucleic acid length and marker effect in pneumococcal transformation. J. Bacteriol. 138:80-86.
24. Lindquist, S. 1986. The heat shock response. Annu. Rev. Biochem. 55:1151-1191.
25. Maurizi, M. R., W. P. Clark, S. H. Kim, and S. Gottesman. 1990. ClpP represents a unique family of serine proteases. J. Biol. Chem. 265:12546-12552.
26. Mitchell, T. J., J. E. Alexander, P. J. Morgan, and P. W. Andrew. 1997. Molecular analysis of virulence factors of Streptococcus pneumoniae. J. Appl. Microbiol. 83:S62-S71.
27. Novak, R., B. Henriques, E. Charpentier, S. Normark, and E. Tuomanen. 1999. Emergence of vancomycin tolerance in Streptococcus pneumoniae. Nature 399:590-593.
28. Polissi, A., A. Pontiggia, G. Feger, M. Altieri, H. Mottl, L. Ferrari, and D. Simon. 1998. Large-scale identification of virulence genes from Streptococcus pneumoniae. Infect. Immun. 66:5620-5629.
29. Pozzi, G., L. Masala, F. Iannelli, R. Manganelli, L. S. Havarstein, L. Piccoli, D. Simon, and D. A. Morrison. 1996. Competence for genetic transformation in encapsulated strains of Streptococcus pneumoniae: two allelic variants of the peptide pheromone. J. Bacteriol. 178:6087-6090.
30. Robertson, G. T., W. L. Ng, J. Foley, R. Gilmour, and M. E. Winkler. 2002. Global transcriptional analysis of clpP mutations of type 2 Streptococcus pneumoniae and their effects on physiology and virulence. J. Bacteriol. 184:3508-3520.
31. Ronda, C., J. L. Garcia, E. Garcia, J. M. Sanchez-Puelles, and R. Lopez. 1987. Biological role of the pneumococcal amidase. Cloning of the lytA gene in Streptococcus pneumoniae. Eur. J. Biochem. 164:621-624.
32. Sambrook, J., E. F. Fritsch, and T. Maniatis. 1989. Molecular cloning: a laboratory manual, 2nd ed. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.
33. Schirmer, E. C., J. R. Glover, M. A. Singer, and S. Lindquist. 1996. HSP100/Clp proteins: a common mechanism explains diverse functions. Trends Biochem. Sci. 21:289-296.
34. Smith, M. D., and W. R. Guild. 1979. A plasmid in Streptococcus pneumoniae. J. Bacteriol. 137:735-739.
35. Spiess, C., A. Beil, and M. Ehrmann. 1999. A temperature-dependent switch from chaperone to protease in a widely conserved heat shock protein. Cell 97:339-347.
36. Squires, C., and C. L. Squires. 1992. The Clp proteins: proteolysis regulators or molecular chaperones? J. Bacteriol. 174:1081-1085.
37. Talbot, U. M., A. W. Paton, and J. C. Paton. 1996. Uptake of Streptococcus pneumoniae by respiratory epithelial cells. Infect. Immun. 64:3772-3777.
38. Tettelin, H., K. E. Nelson, I. T. Paulsen, J. A. Eisen, T. D. Read, S. Peterson, J. Heidelberg, R. T. DeBoy, D. H. Haft, R. J. Dodson, A. S. Durkin, M. Gwinn, J. F. Kolonay, W. C. Nelson, J. D. Peterson, L. A. Umayam, O. White, S. L. Salzberg, M. R. Lewis, D. Radune, E. Holtzapple, H. Khouri, A. M. Wolf, T. R. Utterback, C. L. Hansen, L. A. McDonald, T. V. Feldblyum, S. Angiuoli, T. Dickinson, E. K. Hickey, I. E. Holt, B. J. Loftus, F. Yang, H. O. Smith, J. C. Venter, B. A. Dougherty, D. A. Morrison, S. K. Hollingshead, and C. M. Fraser. 2001. Complete genome sequence of a virulent isolate of Streptococcus pneumoniae. Science 293:498-506.
39. Tomasz, A. 1984. Building and breaking of bonds in the cell wall of bacteria-the role for autolysin, p. 3-12. In C. Nombela (ed.), Microbial cell wall and autolysins. Elsevier Science, Amsterdam, The Netherlands.
40. Tuomanen, E. I., R. Austrian, and H. R. Masure. 1995. Pathogenesis of pneumococcal infection. N. Engl. J. Med. 332:1280-1284.
41. Wickner, S., M. R. Maurizi, and S. Gottesman. 1999. Posttranslational quality control: folding, refolding, and degrading proteins. Science 286:1888-1893.