Purification and molecular characterization of glycylglycine endopeptidase produced by Staphylococcus capitis EPK1

Journal of Bacteriology

Volumn 179, Issue 4, 1997, Pages 1193-1202

  Sugai, Motoyuki ^a   Fujiwara, Tamaki ^a   Akiyama, Tomoko ^a   Ohara, Masaru ^a   Komatsuzawa, Hitoshi ^a   Inoue, Shingo ^a,b   Suginaka, Hidekazu ^a  

^a HIROSHIMA UNIVERSITY   (Japan)

^b UNIFORMED SERVICES UNIVERSITY OF THE HEALTH SCIENCES   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

GLYCYLGLYCINE; LYSOSTAPHIN; PROTEINASE;

AMINO ACID SEQUENCE; ARTICLE; CYTOLYSIS; ENZYME ACTIVITY; ENZYME ANALYSIS; ENZYME PURIFICATION; ENZYME STRUCTURE; MOLECULAR CLONING; NONHUMAN; PRIORITY JOURNAL; PROTEIN DOMAIN; STAPHYLOCOCCUS; SUPERNATANT; TANDEM REPEAT;

STAPHYLOCOCCUS; STAPHYLOCOCCUS AUREUS; STAPHYLOCOCCUS CAPITIS;

EID: 0031046570     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/jb.179.4.1193-1202.1997     Document Type: Article

References (70)

1. Babenko, I., and T. Kulikova. 1984. Interrelation between the activity of the lytic enzyme producer Actinomyces recifensis var. lyticits 2435 and its population variability. Antibiotiki 29:490-495.
2. Birnboim, H. L., and J. Doly. 1979. A rapid alkaline extraction procedure for screening of recombinant plasmid DNA. Nucleic Acid Res. 7:1513-1523.
3. Buist, G., J. Kok, K. J. Leenhouts, M. Dabrowska, G. Venema, and A. J. Haandrikman. 1995. Molecular cloning and nucleotide sequence of the gene encoding the major peptidoglycan hydrolase of Lactococcus lactis, a muramidase needed for cell separation. J. Bacteriol. 177:1554-1563.
4. Bullock, W. O., J. M. Fernandez, and J. M. Short. 1987. XLI-Blue: a high efficiency plasmid transforming recA Escherichia coli strain with beta-galactosidase selection. BioTechniqucs 5:376-379.
5. Burke, M. E., and P. A. Pattee. 1967. Purification and characterization of a staphylolytic enzyme from Pseudomonas aeruginosa. J. Bacteriol. 93:860-865.
6. Carnicero, A., M. A. Falcon, T. B. Mansito, and T. M. Roldan. 1990. A protease with staphylolytic activity from Pseudomonas aeruginosa PAKSI. FEMS Microbiol. Lett. 58:171-175.
7. Carnicero, A., T. B. Mansito, J. M. Roldan, and M. A. Falcon. 1990. Staphylolytic enzyme from Pseudomonas aeruginosa. Arch. Microbiol. 154:37-41.
8. Chatterjee, A. N., W. Wong, F. E. Young, and R. W. Gilpin. 1976. Isolation and characterization of a mutant of Staphylococcus aureus H. J. Bacteriol. 168:961-967.
9. Coleman, J. E. 1992. Zinc proteins: enzymes, storage proteins, transcription factors, and replication proteins. Annu. Rev. Biochem. 61:897-946.
10. Coles, N. W., C. M. Gilbo, and A. T. Broad. 1969. Purification, properties and mechanism of action of a staphylolytic enzyme produced by Aeromonas hydrophilia. Biochem. J. 111:7-15.
11. Dehart, H. P., H. E. Heath, L. S. Heath, P. A. Leblanc, and G. L. Sloan. 1995. The lysostaphin endopeptidase resistance gene (epr) specifies modification of peptidoglycan cross bridges in Staphylococcus simulans and Staphylococcus aureus. Appl. Environ. Microbiol. 61:1475-1479.
12. Fischer, W. 1994. Lipoteichoic acids and lipoglycans, p. 199-215. In J.-M. Ghuysen and R. Hakenbeck (ed.). Bacterial cell wall. Eisevier Science B. V., Amsterdam, The Netherlands.
13. Fleischmann, R. D., M. D. Adams, O. White, R. A. Clayton, E. F. Kirkness, A. R. Kerlavage, C. J. Bult, J. Tomb, B. A. Dougherty, J. M. Merrick, K. McKenney, G. Sutton, W. FitzHugh, C. A. Fields, J. D. Gocayne, J. D. Scott, R. Shirley, L. Liu, A. Glodek, J. M. Kelley, J. F. Weidman, C. A. Phillips, T. Spriggs, E. Hedblom, M. D. Cotton, T. R. Utterback, M. C. Hanna, D. T. Nguyen, D. M. Saudek, R. C. Brandon, L. D. Fine, J. L. Fritchman, J. L. Fuhrmann, N. S. M. Geoghagen, C. L. Gnehm, L. A. McDonald, K. V. Small, C. M. Fraser, H. O. Smith, and J. C. Venter. 1995. Whole-genome random sequencing and assembly of Haemophilus influenzae Rd. Science 269:496-512.
14. Garcia, J. L., E. Diaz, A. Romero, and P. Garcia. 1994. Carboxy-terminal deletion analysis of the major pneumococcal autolysin. J. Bacteriol. 176:4066-4072.
15. Ghuysen, J., D. J. Tipper, and J. L. Strominger. 1966. Enzymes that degrade bacterial cell walls. Methods Enzymol. 8:685-699.
16. Gustin, J. K., E. Kessler, and D. E. Ohman. 1996. A substitution at His-120 in the LasA protease of Pseudomonas aeruginosa blocks enzymatic activity without affecting propeptide processing or extracellular secretion. J. Bacteriol. 178:6608-6617.
17. Hash, H. J. 1963. Purification and properties of staphylolytic enzymes from Chalaropsis sp. Arch. Biochem. Biophys. 102:379-388.
18. Heath, H. E., L. S. Heath, J. D. Nitterauer, K. E. Rose, and G. L. Sloan. 1989. Plasmid-encoded lysostaphin endopeptidase resistance of Staphylococcus simulans biovar staphylolyticus. Biochem. Biophys. Res. Commun. 160:1106-1109.
19. Heijne, G. 1986, A new method for predicting signal sequence cleavage sites. Nucleic Acids Res. 14:4683-4690.
20. Heinrich, P., R. Rosenstein, M. Böhmer, P. Sonner, and F. Götz. 1987. The molecular organization of the lysostaphin gene and its sequences repeated in tandem. Mol. Gen. Genet. 209:563-569.
21. Häse, C. C., and R. A. Finkelstein. 1993. Bacterial extracellular zinc-containing metalloproteases. Microbiol. Rev. 57:823-837.
22. Ichikawa, J. K., C. Li, J. Fu, and S. Clarke. 1994. A gene at 59 minutes on the Escherichia coli chromosome encodes a lipoprotein with unusual amino acid repeat sequences. J. Bacteriol. 176:1630-1638.
23. Iriarte, M., I. Stainier, and G. R. Cornells. 1995. The ipoS gene from Yersinia enterocolitica and its influence on expression of virulence factors. Infect. Immun. 63:1840-1847.
24. Iversen, O., and A. Grov. 1973. Studies on lysostaphin. Separation and characterization of three enzymes. Eur. J. Biochem. 38:293-300.
25. Janda, J. M., M. Reitano, and E. J. Bottone. 1984. Biotyping of Aeromonas isolates as a correlate to delineating a species-associated disease spectrum. J. Clin. Microbiol. 19:44-47.
26. Karow, M., and C. Georgopoulos. 1992. Isolation and characterization of the Escherichia coli msbB gene, a multicopy suppressor of null mutations in the high-temperature requirement gene htrB. J. Bacteriol. 174:702-710.
27. Kato, K., S. Kotani, T. Matsubara, J. Jogami, S. Haashimoto, M. Chimori, and I. Kazekawa. 1962. Lysis of Staphylococcus aureus cell wall by a lytic enzyme purified from culture supernatant of Flavobacterium species. Biken J. 5:155-179.
28. Kessler, E., M. Safrin, J. C. Olson, and D. E. Ohman. 1993. Secreted LasA of Pseudomonas aeruginosa is a staphylolytic protease. J. Biol. Chem. 268:7503-7508.
29. Kovach, M. E., K. J. Hughes, K. D. Everiss, and K. M. Peterson. 1994. Identification of a ToxR-activalcd gene. tagE, that lies within the accessory colonization factor gene cluster of Vibrio cholerae O395. Gene 148:91-95.
30. Lange, R., and R. Hengge-Aronis. 1994. The nlpD gene is located in an operon with rpoS on the Escherichia coli chromosome and encodes a novel lipoprotein with a potential function in cell wall formation. Mol. Microbiol. 13:733-743.
31. LeClerc, D., and A. Asselin. 1989. Detection of bacterial cell wall hydrolases after denaturing polyacrylamide gel electrophoresis. Can. J. Microbiol. 35:749-753.
32. Li, S. L., S. Norioka, and F. Sakiyama. 1990. Molecular cloning and nucleotide sequence of the β-lytic protease gene from Achromobacter liticus. J. Bacteriol. 172:6506-6511.
33. Matsudaira, P. 1987. Sequence from picomole quantities of proteins electroblotted onto polyvinylidene membranes. J. Biol. Chem. 262:10035-10038.
34. Nakai, K., A. Kidera, and M. Kanehisa. 1988. Cluster analysis of amino acid indices for prediction of protein structure and function. Protein Eng. 2:93-100.
35. Nord, C. E., L. Sjoberg, T. Wadstrom, and B. Wretlind. 1975. Characterization of three Aeromonas and nine Psedomonas species by extracellular enzymes and hemolysis. Med. Microbiol. Immunol. 161:79-87.
36. Nord, C. E., T. Wadström, K. Dornbusch, and B. Wretlind. 1975. Extracellular proteins in five clostridial species from human infections. Med. Microbiol. Immunol. 161:145-154.
37. Novick, R. P. 1990. The staphylococcus as a molecular genetic system, p. 1-37. In P. R. Novick (ed.). Molecular biology of the staphylococci. VCH Publishers, Inc., New York, N.Y.
38. Oshida, T., M. Sugai, H. Komatsuzawa, Y.-M. Hong, H. Suginaka, and A. Tomasz, 1995. A Staphylococcus aureus autolysin that has an N-acetylmuramoyl-L-alanine amidasc domain and an endo-β-N-acetylglucosaminidase domain: cloning, sequence analysis, and characterization. Proc. Natl. Acad. Sci. USA 92:285-289.
39. Park, P. W., R. M. Senior, G. L. Griffin, T. J. Broekelmann, M. S. Mudd, and R. P. Mecham. 1995. Binding and degradation of elastin by the staphylolytic enzyme lysostaphin. Int. J. Biochem. Cell Biol. 27:139-146.
40. Park, S., and D. R. Galloway. 1995. Purification and characterization of LasD: second staphylolytic proteinase produced by Pseudomonas aeruginosa. Mol. Microbiol. 16:263-270.
41. Recsei, P. A., A. D. Gruss, and R. P. Novick, 1987. Cloning, sequence, and expression of the lysostaphin gene from Staphylococcus simulons. Proc. Natl. Acad. Sci. USA 84:1127-1131.
42. Robbe-Saule, V., C. Coynault, and F. Norel. 1995. The live oral typhoid vaccine Ty21a is a rpoS mutant and is susceptible to various environmental stresses. FEMS Microbiol. Lett. 126:171-176.
43. Sambrook, J., T. Maniatis, and E. F. Fritsch. 1989. Molecular cloning: a laboratory manual. Cold Spring Harbor Laboratory Press, Cold Spring Harbor. N.Y.
44. Sanger, F., S. Nicklen, and A. R. Coulson. 1977. DNA sequencing with chain-terminating inhibitors. Proc. Natl. Acad. Sci. USA 74:5463-5467.
45. Schindler, C. A., and V. T. Schuhardt. 1964. Lysostaphin: a new bacteriolytic agent for the Staphylococcus. Proc. Natl. Acad. Sci. USA 51:414-421.
46. Schindler, C. A., and V. T. Schuhardt. 1965 Purification and properties of lysostaphin - a lytic agent for Staphylococcus aureus. Biochem. Biophys. Acta 97:242-250.
47. Schleifer, K. H. 1986. Gram-positive cocci, p. 1022-1023. In P. H. A. Sneath, N. S. Mair, and J. G. Holt (ed.), Bergey's manual of systematic bacteriology. Williams & Wilkins. Baltimore. Md.
48. Shad, P. A., and B. H. Iglewski. 1988. Nucleotide sequence and expression in Escherichia coli of the Pseudomonas aeruginosa lasA gene. J. Bacteriol. 170:2784-2789.
49. Smith, P. K., R. I. Krohn, G. T. Hermanson, A. K. Mallia, F. H. Gartner, M. D. Provenzano, E. K. Fujinioto, N. M. Geoke, B. J. Olson, and D. C. Kienk, 1985. Measurement of protein bicinchoninic acid. Anal. Biochem. 150:76-85.
50. Smith, T. J., and S. J. Foster. 1995. Characterization of the involvement of two compensatory autolysins in mother cell lysis during sporulation of Bacillus subtilis 168. J. Bacteriol. 177:3855-3862
51. Sugai, M., T. Akiyama, H. Komatsuzawa, Y. Miyake, and H. Suginaka. 1990. Characterization of sodium dodecyl sulfate-stable Staphylococcus aureus bacteriolytic enzymes by polyacrylamide gel elcctrophoresis. J. Bacteriol. 172:6494-6498.
52. Sugai, M., T. Akiyama, Y. Miyake, E. Ishida, and H. Suginaka. 1990. Rapid purification method of lysostaphin for analysis of cell-wall proteins. J. Microbiol. Methods 12:133-138.
53. Sugai, M., H. Koike, Y. Hong, Y. Miyake, R. Nogami, and H. Suginaka. 1989. Purification of a 51 kDa endo-β-N-acetylglucosaminidase from Staphylococcus aureus. FEMS Microbiol. Lett. 61:267-272.
54. Sugai, M., H. Komatsuzawa, T. Akiyama, Y.-M. Hong, T. Oshida, Y. Miyake, T. Yamaguchi, and H. Suginaka. 1995. Identification of endo-β-N-acetylglucosaminidase and N-acetylmuramyl-L-alanine amidase as cluster-dispersing enzymes in Staphyhcoccus aureus. J. Bacteriol. 177:1491-1496.
55. Sugai, M., H. Komatsuzawa, K. Ooku-Inomata, Y. Miyake, E. Ishida, and H. Suginaka. 1994. Isolation and characterization of Staphylococcus aureus mutants which form altered cell clusters. Microbiol. Immunol. 38:995-999.
56. Suginaka, H., S. Kashiba, T. Amano, S. Kotani, and T. Imanishi. 1967. Purification and properties of a staphylolytic factor produced by a strain of Staphylococcus epidermidis. Biken J. 10:109-120.
57. Tanaka, K., and H. Takahashi. 1994. Cloning, analysis and expression of an rpoS homologue gene from Pseudomonas aeruginosa. Gene 150:81-85.
58. Theisen, M., C. R. Rioux, and A. A. Potter. 1993. Molecular cloning, nucleotide sequence, and characterization of IppB, encoding an antigenic 40-kilodalton lipoprotein of Haemophilus somnus. Infect. Immun. 61:1793-1798.
59. Thompson, J. S., and G. D. Shockman. 1969. A modification of the Park and Johnson reducing sugar determination suitable for the assay of insoluble materials: its application to bacterial cell wall. Anal. Biochem. 22:260-268.
60. Trayer, H. R., and C. E. Buckley III. 1970. Molecular properties of lysostaphin, a bacteriolytic agent specific for Staphyhcoccus aureus. J. Biol. Chem. 245:4842-4846.
61. Vallee, B. L., and D. S. Auld. 1990. Zinc coordination, function, and structure of zinc enzymes and other proteins. Biochemistry 29:5647-5659.
62. Wadström, T., and O. Vesterberg. 1971. Studies on endo-beta-N-acetylglucosaminidasc, staphylolytic peptidastr, and N-acetylmuramyl-L-alanine amidase in lysostaphin and from Staphylococcus aureus. Acta Pathol. Microbiol. Scand. 79:248-264.
63. Wang, X., B. J. Wilkinson, and R. K. Jayaswal. 1991. Sequence analysis of a Staphylococcus aureus gene encoding a peptidoglycan hydrolase activity. Gene 102:105-109.
64. Ward, J. B., and H. R. Perkins. 1968. The purification and properties of two staphylolytic enzymes from Streptomyces griseus. Biochem. J. 106:69-76.
65. Warren, R., M. Rogolsky, B. B. Wiley, and L. A. Glasgow. 1974. Effect of ethidium bromide on elimination of exfoliative toxin and bacteriocin production in Staphylococcus aureus. J. Bacteriol. 118:980-985.
66. Whitaker, D. R. 1965. Lytic enzymes of Sorangium sp., a comparison of proteolytic properties of the alpha-lytic and beta-lytic proteases. Can. J. Biochem. 43:1935-1954.
67. Wren, B. W. 1991. A family of clostridial and streptococcal ligand-binding proteins with conserved C-terminal repeat sequences. Mol. Microbiol. 5:797-803.
68. Wretlind, B., L. Heden, and T. Wadström. 1973. Formation of extracellular haemolysin by Aeromonas hydrophilia in relation to protease and staphylolytic enzyme. J. Gen. Microbiol. 78:57-65.
69. Yanisch-Perron, C., J. Vieira, and J. Messing. 1985. Improved M13 phage cloning vectors and host strains: nucleotide sequences of the M13mp18 and pUC19 vectors. Gene 33:103-119.
70. Yoshimoto, T., and D. Tsuru. 1972. Studies in bacteriolytic enzymes. II. Purification and some properties of two types of staphyloiytic enzymes from Streptomyces griseus. J. Biochem. 72:379-390.