Role of the Enterococcus faecalis Ge1E protease in determination of cellular chain length, supernatant pheromone levels, and degradation of fibrin and misfolded surface proteins

Journal of Bacteriology

Volumn 185, Issue 12, 2003, Pages 3613-3623

  Waters, Christopher M ^a   Antiporta, Michelle H ^a   Murray, Barbara E ^b   Dunny, Gary M ^a  

^a UNIVERSITY OF MINNESOTA MEDICAL SCHOOL   (United States)

^b UNIVERSITY OF TEXAS MEDICAL SCHOOL   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

AUTOLYSIN; BACTERIAL PROTEIN; FIBRIN; GELATINASE; MUTANT PROTEIN; PHEROMONE; VIRULENCE FACTOR; ZINC;

ARTICLE; AUTOLYSIS; CELL DENSITY; CELL STRUCTURE; ENTEROCOCCUS FAECALIS; FIBRIN POLYMERIZATION; FIBRINOLYSIS; NONHUMAN; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN DEGRADATION; PROTEIN EXPRESSION; PROTEIN FOLDING; PROTEIN FUNCTION; PROTEIN STABILITY; STREPTOCOCCUS PYOGENES; SUPERNATANT;

BACTERIAL PROTEINS; ENTEROCOCCUS FAECALIS; ENZYME ACTIVATION; FIBRIN; GELATINASES; GENES, BACTERIAL; MEMBRANE PROTEINS; MUTATION; N-ACETYLMURAMOYL-L-ALANINE AMIDASE; OLIGOPEPTIDES; PHEROMONES; STREPTOCOCCUS PYOGENES; TRANSFORMATION, BACTERIAL; VIRULENCE;

ANIMALIA; BACTERIA (MICROORGANISMS); ENTEROCOCCUS FAECALIS; POSIBACTERIA; STREPTOCOCCUS PYOGENES;

EID: 0037946947     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/JB.185.12.3613-3623.2003     Document Type: Article

References (42)

1. Bae, T., B. Kozlowicz, and G. M. Dunny. 2002. Two targets in pCF10 DNA for PrgX binding: their role in production of Qa and prgX mRNA and in regulation of pheromone-inducible conjugation. J. Mol. Biol. 315:995-1007.
2. Beliveau, C., C. Potvin, J. Trudel, A. Asselin, and G. Bellemare. 1991. Cloning, sequencing, and expression in Escherichia coli of a Streptococcus faecalis autolysin. J. Bacteriol. 173:5619-5623.
3. Bleiweis, A. S., and L. N. Zimmerman. 1964. Properties of proteinase from Streptococcus faecalis var. liquefaciens. J. Bacteriol. 98:653-659.
4. Bryan, E. M., T. Bae, H. Kleerebezem, and G. M. Dunny. 2000. Improved vectors for nisin-controlled expression in gram-positive bacteria. Plasmid 44:183-190.
5. Buttaro, B. A., M. H. Antiporta, and G. M. Dunny. 2000. Cell-associated pheromone peptide (cCF10) production and pheromone inhibition in Enterococcus faecalis. J. Bacteriol. 182:4926-4933.
6. Cleary, P. P., E. L. Kaplan, J. P. Handley, A. Wlazlo, M. H. Kim, A. R. Hauser, and P. M. Schlievert. 1992. Clonal basis for resurgence of serious Streptococcus pyogenes disease in the 1980s. Lancet 339:518-521.
7. Coque, T. M., J. E. Patterson, J. M. Steckelberg, and B. E. Murray. 1995. Incidence of hemolysin, gelatinase, and aggregation substance among enterococci isolated from patients with endocarditis and other infections and from feces of hospitalized and community-based persons. J. Infect. Dis. 171:1223-1229.
8. Dolinger, D. L., L. Daneo-Moore, and G. D. Shockman. 1989. The second peptidoglycan hydrolase of Streptococcus faecium ATCC 9790 covalently binds penicillin. J. Bacteriol. 171:4355-4361.
9. Dolinger, D. L., V. L. Schramm, and G. D. Shockman. 1988. Covalent modification of the β-1,4-N-actylmuramoylhydrolase of Streptococcus faecium with 5-mercaptouridine monophosphate. Proc. Natl. Acad. Sci. USA 85:6667-6671.
10. Dunny, G. M., B. L. Brown, and D. B. Clewell. 1978. Induced cell aggregation and mating in Streptococcus faecalis: evidence for a bacterial sex pheromone. Proc. Natl. Acad. Sci. USA 75:3479-3483.
11. Dunny, G. M., M. Yuhasz, and E. Ehrenfeld. 1982. Genetic and physiological analysis of conjugation in Streptococcus faecalis. J. Bacteriol. 151:855-859.
12. Fontana, R. A., M. Boaretti, A. Grossato, E. A. Tonin, M. M. Lleo, and G. Satta. 1990. Paradoxical response of Enterococcus faecalis to the bactericidal activity of penicillin is associated with reduced activity of one autolysin. Antimicrob. Agents Chemother. 34:314-320.
13. Galli, D., F. Lottspeich, and R. Wirth. 1990. Sequence analysis of Enterococcus faecalis aggregation substance encoded by the sex pheromone plasmid pAD1. Mol. Microbiol. 4:895-904.
14. Galloway, D. R. 1991. Pseudomonas aeruginosa elastase and elastolysis revisited: recent developments. Mol. Microbiol. 5:2315-2321.
15. Garcia, P., M. P. Gonzalez, E. Garcia, R. Lopez, and J. L. Garcia. 1999. LytB, a novel pneumococcal murein hydrolase essential for cell separation. Mol. Microbiol. 31:1275-1281.
16. Hase, C. C., and R. A. Finkelstein. 1993. Bacterial extracellular zinc-containing metalloproteases. Microbiol. Rev. 57:823-837.
17. Hirt, H., S. L. Erlandsen, and G. M. Dunny. 2000. Heterologous inducible expression of Enterococcus faecalis pCF10 aggregation substance Asc10 in Lactococcus lactis and Streptococcus gordonii contributes to cell hydrophobicity and adhesion to fibrin. J. Bacteriol. 182:2299-2306.
18. Hirt, H., P. M. Schlievert, and G. M. Dunny. 2002. In vivo induction of virulence and antibiotic resistance transfer in Enterococcus faecalis mediated by the sex pheromone -sensing system of pCF10. Infect. Immun. 70:716-723.
19. Jettt, B. D., M. M. Huycke, and M. S. Gilmore. 1994. Virulence of enterococci. Clin. Microbiol. Rev. 7:462-478.
20. Kawamura, T., and G. D. Shockman. 1983. Purification and some properties of the endogenous, autolytic N-acetylmuramolylhydrolase of Streptococcus faecium, a bacterial glycoenzyme. J. Biol. Chem. 258:9514-9521.
21. Kuipers, O. P., M. M. Beerthuizen, R. J. Siezen, and W. M. de Vos. 1993. Characterization of the nisin gene cluster nisABTCIPR of Lactococcus lactis: requirement of expression of the nisA and nisI genes for development of immunity. Eur. J. Biochem. 216:281-291.
22. Makinen, P., D. B. Clewell, F. An, and K. K. Makinen. 1989. Purification and substrate specificity of a strongly hydrophobic extracellular metalloendopeptidase ("gelatinase") from Streptococcus faecalis (strain OG1-10.). J. Biol. Chem. 264:3325-3334.
23. Makinen, P., and K. K. Makinen. 1994. The Enterococcus faecalis extracellular metalloendopeptiadase (EC 3.4.24.30; coccolysin) inactivates human endothelin at bonds involving hydrophobic amino acid residues. Biochem. Biophys. Res. Commun. 200:981-985.
24. McCormick, J., H. Hirt, G. M. Dunny, and P. M. Schlievert. 2000. Pathogenic mechanisms of enterococcal endocarditis. Curr. Infect. Dis. Rep. 2:315-321.
25. McCormick, J. K., H. Hirt, C. M. Waters, T. J. Tripp, G. M. Dunny, and P. M. Schlievert. 2001. Antibodies to a surface-exposed, N-terminal domain of aggregation substance are not protective in the rabbit model of Enterococcus faecalis infective endocarditis. Infect. Immun. 69:3305-3314.
26. Miyoshi, S., and S. Shinoda. 2000. Microbial metalloproteases and pathogenesis. Microb. Infect. 2:91-98.
27. Pakula, R., and W. Walczak. 1963. On the nature of transformable streptococci. J. Gen. Microbiol. 31:125-133.
28. Poquet, I., V. Saint, E. Seznec, N. Simoes, A. Bolotin, and A. Gruss. 2000. HtrA in the unique surface housekeeping protease in Lactococcus lactis and is required for natural protein processing. Mol. Microbiol. 35:1042-1051.
29. Qin, X. 2000. Identification and characterization of virulence in Enterococcus faecalis. Ph.D. thesis. University of Texas Graduate School of Biomedical Sciences, Houston.
30. Qin, X., K. V. Singh, G. M. Weinstock, and B. M. Murray. 2000. Effects of Enterococcus faecalis fsr genes on production of gelatinase and a serine protease and virulence. Infect. Immun. 68:2579-2586.
31. Qin, X., K. V. Singh, G. M. Weinstock, and B. M. Murray. 2001. Characterization of fsr. a regulator controlling expression of gelatinase and serine protease in Enterococcus faecalis OG1RF. J. Bacteriol. 183:3372-3382.
32. Qin, X., K. V. Singh, Y. Xu, G. M. Weinstock, and B. E. Murray. 1998. Effect of disruption of a gene encoding an autolysin of Enterococcus faecalis OG1RF. Antimicrob. Agents Chemother. 42:2883-2888.
33. Rasmussen, M., and L. Bjorck. 2002. Proteolysis and its regulation at the surface of Streptococcus pyogenes. Mol. Microbiol. 43:537-544.
34. Sanchez-Puelles, J. M., C. Ronda, J. L. Garcia, P. Garcia, R. Lopez, and E. Garcia. 1986. Searching for autolysin functions: characterization of a pneumococcal mutant deleted in the lytA gene. Eur. J. Biochem. 158:289-293.
35. Schlievert, P. M., P. J. Gahr, A. P. Assimacopoulos, M. M. Dinges, J. A. Stoehr, H. Hirt, and G. M. Dunny. 1998. Aggregation and binding substances enhance pathogenicity in rabbit models of Enterococcus faecalis endocarditis. Infect. Immun. 66:218-223.
36. Shockman, G. D., and M. C. Cheney. 1969. Autolytic enzyme system of Streptococcus faecalis (V). J. Bacteriol. 98:1199-1207.
37. Sifri, C. D., E. Mylonakis, K. V. Singh, X. Qin, D. A. Garsin, B. M. Murray, F. M. Ausubel, and S. B. Calderwood. 2002. Virulence effect of Enterococcus faecalis protease genes and the quorum-sensing locus fsr in Caenorhabditis elegans and mice. Infect. Immun. 70:5647-5650.
38. , Singh, K. V., X. Qin, G. M. Weinstock, and B. M. Murray. 1998. Generation and testing of mutants of Enterococcus faecalis in a mouse peritonitis model. J. Infect. Dis. 178:1416-1420.
39. Su, Y. A., M. C. Sulavik, P. He, K. K. Makinen, P. Makinen, S. Fiedler, R. Wirth, and D. B. Clewell. 1991. Nucleotide sequence of the gelatinase gene (gelE) from Enterococcus faecalis subsp. liquefaciens. Infect. Immun 59:415-420.
40. Tomasz, A. 1968. Biological consequence of the replacement of choline by ethanolamine in the cell wall of pneumococcus: chain formation, loss of transformability, and loss of autolysis. Proc. Natl. Acad. Sci. USA 59:86-93.
41. Waters, C. M., and G. M. Dunny. 2001. Analysis of functional domains of the Enterococcus faecalis pheromone-induced surface protein aggregation substance. J. Bacteriol. 183:5659-5667.
42. Yother, J., K. Leopold, J. White, and W. Fischer. 1998. Generation and properties of a Streptococcus pneumoniae mutant which does not require choline or analogs for growth. J. Bacteriol. 180:2093-2101.