Catalase deficiency in Staphylococcus aureus subsp. anaerobius is associated with natural loss-of-function mutations within the structural gene

Microbiology

Volumn 146, Issue 2, 2000, Pages 465-475

  Sanz, Rosario ^a   Marín, Irma ^b   Ruiz Santa Quiteria, Jose A ^a   Orden, Jose A ^a   Cid, Dolores ^a   Diez, Rosa M ^a   Souad Silhadi, K ^c   Amils, Ricardo ^b   De La Fuente, Ricardo ^a  

^a UNIVERSIDAD COMPLUTENSE DE MADRID   (Spain)

^b UNIVERSIDAD AUTÓNOMA DE MADRID   (Spain)

^c UPRES EA 1655 Lab Bacteriol F   (France)

Author keywords

Catalase; Catalase gene; Staphylococcus aureus subsp. anaerobius

Indexed keywords

BACTERIAL ENZYME; CATALASE;

ARTICLE; BACTERIAL GENE; CATALASE DEFICIENCY; ENZYME ACTIVITY; ESCHERICHIA COLI; GENE DELETION; GENE MUTATION; MISSENSE MUTATION; MOLECULAR WEIGHT; NONHUMAN; NORTHERN BLOTTING; NUCLEOTIDE SEQUENCE; OPEN READING FRAME; POLYMERASE CHAIN REACTION; PRIORITY JOURNAL; SOUTHERN BLOTTING; STAPHYLOCOCCUS AUREUS; START CODON; STRUCTURAL GENE;

ESCHERICHIA COLI; STAPHYLOCOCCUS AUREUS;

EID: 0033953873     PISSN: 13500872     EISSN: None     Source Type: Journal    
DOI: 10.1099/00221287-146-2-465     Document Type: Article

References (33)

1. Ausubel, F. M., Brent, R., Kingston, R. E., Moore, D. D., Seidman, J. G., Smith, J. A. & Struhl, K. (1991). Current Protocols in Molecular Biology. New York: Wiley.
2. Clare, D. A., Duong, M. N., Darr, D., Archibald, F. & Fridovich, I. (1984). Effects of molecular oxygen on detection of superoxide radical with nitroblue tetrazolium and on activity stains for catalase. Anal Biochem 140, 532-537.
3. De la Fuente, R. & Suarez, G. (1985). Respiratory deficient Staphylococcus aureus as the aetiological agent of 'abscess disease'. Zentbl Vet Med B 32, 397-406.
4. De la Fuente, R., Suarez, G. & Schleifer, K. H. (1985). Staphylococcus aureus subsp. anaerobius subsp. nov., the causal agent of abscess disease of sheep. Int J Syst Bacteriol 35, 99-102.
5. De la Fuente, R., Götz, F. & Shleifer, K. H. (1987). Comparative biochemical studies on aerobic mutants of Staphylococcus aureus subsp. anaerobius. Syst Appl Microbiol 9, 29-33.
6. De la Fuente, R., Ruiz Santa Quiteria, J. A., Cid, D., Domingo, M. & Suarez, G. (1993). Experimental intramammary infection of ewes with Staphylococcus aureus subsp anaerobius. Res Vet Sci 54, 221-226.
7. Devereux, J., Haeberli, P. & Smithies, O. (1984). A comprehensive set of sequence analysis programs for the VAX. Nucleic Acids Res 12, 387-395.
8. Fita, I. & Rossmann, M. G. (1985a). Tha NADPH binding site on beef liver catalase. Proc Natl Acad Sci USA 82, 1604-1608.
9. Fita, I. & Rossmann, M. G. (1985b). The active center of catalase. J Mol Biol 185, 21-37.
10. Gouet, P., Jouve, H. M. & Dideberg, O. (1995). Crystal structure of Proteus mirabilis PR catalase with and without bound NADPH. J Mol Biol 249, 933-954.
11. Haas, A. & Brehm, K. (1993). Superoxide dismutases and catalases: biochemistry, molecular biology and some biomedical aspects. Genet Eng Biotechnol 13, 243-269.
12. Higuchi, R. (1989). Using PCR to engineer DNA. In PCR Technology. Principles and Applications for DNA Amplification, pp. 61-70. Edited by H. A. Erlich. New York: Macmillan.
13. Horwitz, M. S. Z. & Loeb, L. A. (1990). Structure-function relationship in Escherichia coli promoter DNA. Prog Nucleic Acid Res Mol Biol 38, 137-164.
14. Kanafani, H. & Martin, S. E. (1985). Catalase and superoxide dismutase activities in virulent and nonvirulent Staphylococcus aureus isolates. J Clin Microbiol 21, 607-610.
15. Klotz, M. G., Klassen, G. R. & Loewen, P. C. (1997). Phylogenetic relationships among prokaryotic and eukaryotic catalases. Mol Biol Evol 14, 951-958.
16. Kornblum, J. S., Projan, S. J., Moghazeh, S. L. & Novick, R. P. (1988). A rapid method to quantitate nonlabeled RNA species in bacterial cells. Gene 63, 75-85.
17. Loewen, P. C. (1992). Regulation of bacterial catalase synthesis. In Molecular Biology of Free Radical Scavenging Systems, pp. 96-116. Edited by J. Scandalios. Cold Spring Harbor, NY: Cold Spring Harbor Laboratory.
18. Mandell, G. L. (1975). Catalase, superoxide dismutase, and virulence of Staphylococcus aureus. In vivo and in vitro studies with emphasis on staphylococcal-leucocyte interaction. J Clin Invest 55, 561-566.
19. Melik-Adamyan, W. R., Barynin, V. V., Vagin, A. A., Borisov, V. V., Vainshtein, B. K., Fita, I., Murthy, M. R. N. & Rossmann, M. G. (1986). Comparison of beef liver and Penicillium vitale catalases. J Mol Biol 188, 63-72.
20. Murthy, M. R. N., Reid, T. J., III, Sicignano, A., Tanaka, N. & Rossmann, M. G. (1981). Structure of beef liver catalase. J Mol Biol 152, 465-499.
21. Rocha, E. R. & Smith, C. J. (1995). Biochemical and genetic analyses of a catalase from the anaerobic bacterium Bacteroides fragilis. J Bacteriol 177, 3111-3119.
22. Ruiz Santa Quiteria, J. A., Cid, D., Bellahsene, R., Suarez, G. & De la Fuente, R. (1992). Polyclonal antibodies against Staphylococcus aureus ATCC 12600 catalase do not recognize any protein in cellular extracts from S. aureus subsp. anaerobius. FEMS Microbiol Lett 72, 173-176.
23. Rupprecht, M. & Schleifer, K. H. (1979). A comparative immunological study of catalases from coagulase-positive staphylococci. Arch Microbiol 120, 53-56.
24. Sambrook, J., Fritsch, E. F. & Maniatis, T. (1989). Molecular Cloning: a Laboratory Manual, 2nd edn. Cold Spring Harbor, NY: Cold Spring Harbor Laboratory.
25. Sanger, F., Nicklen, S. & Coulson, A. R. (1977). DNA sequencing with chain-terminating inhibitors. Proc Natl Acad Sci USA 74, 5463-5467.
26. Sinha, A. K. (1972). Colorimetric assay of catalase. Anal Biochem 47, 389-394.
27. Switala, J., Triggs-Raine, B. L. & Loewen, P. C. (1990). Homology among bacterial catalase genes. Can J Microbiol 36, 728-731.
28. Timoney, J. F., Gillespie, J. H., Scott, F. W. & Baslough, J. E. (1988). The staphylococci. In Hagan and Bruner's Microbiology and Infectious Diseases of Domestic Animals, 8th edn, pp. 171-180. Ithaca & London: Comstock Publishing.
29. Vandenesch, F., Lebeau, C., Bes, M., McDevitt, D., Greenland, T., Novick, R. P. & Etienne, J. (1994). Coagulase deficiency in clinical isolates of Staphylococcus aureus involves both transcriptional and post-transcriptional defects. J Med Microbiol 40, 344-349.
30. Von Ossowski, I., Hausner, G. & Loewen, P. C. (1993). Molecular evolutionary analysis based on the amino acid sequence of catalase. J Mol Evol 37, 71-76.
31. Wada, K., Wada, Y., Ishibashi, F., Gojobori, T. & Ikemura, T. (1992). Codon usage tabulated from the GenBank genetic sequence data. Nucleic Acids Res 20, 2111-2118.
32. Watson, D. L. (1988). Vaccination againts experimental staphylococcal mastitis in ewes. Res Vet Sci 45, 16-21.
33. Yanisch-Perron, C., Vieira, J. & Messing, J. (1985). Improved M13 phage cloning vectors and host strains: nucleotide sequences of the M13, mp18 and pUC19 vectors. Gene 33, 103-119.