Characteristics of the biologically active 35-kDa metalloprotease virulence factor from Listeria monocytogenes

Journal of Applied Microbiology

Volumn 88, Issue 1, 2000, Pages 132-141

  Coffey, A ^a,c   Van Den Burg, B ^b   Veltman, R ^b   Abee, Tjakko ^a  

^a WAGENINGEN UNIVERSITY   (Netherlands)

^b UNIVERSITY OF GRONINGEN   (Netherlands)

^c ANIMAL AND GRASSLAND RESEARCH AND INNOVATION CENTRE   (Ireland)

Author keywords

[No Author keywords available]

Indexed keywords

AFFINITY CHROMATOGRAPHY; BACTERIOLOGY; CASEIN; CHEMICAL DETECTION; ENZYME ACTIVITY; HIGH PERFORMANCE LIQUID CHROMATOGRAPHY; PATHOGENS; SUBSTRATES;

CELL SPREADS; ENVIRONMENTAL PARAMETER; EXTRACELLULAR PROTEASE; INTRACELLULAR PATHOGENS; L.MONOCYTOGENES; LISTERIA MONOCYTOGENES; METALLO-PROTEASE; PHOSPHATIDYL CHOLINE; PHOSPHOLIPASE C; VIRULENCE FACTORS;

LISTERIA;

ACTIN; CASEIN; METALLOPROTEINASE; PHOSPHOLIPASE; PROTEINASE; THERMOLYSIN; VIRULENCE FACTOR;

ARTICLE; BACILLUS SUBTILIS; BACTERIAL VIRULENCE; CELL SPREADING; ENZYME ANALYSIS; ENZYME ISOLATION; ENZYME SPECIFICITY; ENZYME SYNTHESIS; LISTERIA MONOCYTOGENES; NONHUMAN;

BACILLUS SUBTILIS; BACTERIA (MICROORGANISMS); EUKARYOTA; LISTERIA MONOCYTOGENES; POSIBACTERIA;

EID: 0034107664     PISSN: 13645072     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1365-2672.2000.00941.x     Document Type: Article

References (42)

1. Amezaga, M., Davidson, I., McLagan, D., Verheul, A., Abee, T. and Booth, I.R. (1995) The role of peptide metabolism in the growth of Listeria monocytogenes ATCC 23074 at high osmolarity. Microbiology 141, 41-49.
2. Beumer, R.R., te Giffel, M.C., Cox, L.J., Rombouts, F.M. and Abee, T. (1994) Effect of exogenous proline, betaine and carnitine on growth of Listeria monocytogenes in a minimal medium. Applied and Environmental Microbiology 60, 1359-1363.
3. Beynon, R.S. and Boud, J.S., eds. (1989) Proteolytic Enzymes: A Practical Approach. Oxford: IRL Press.
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. Analytical Biochemistry 72, 248-254.
5. van den Burg, B., Eijsink, V.G.H., Stulp, B.K. and Venema, G. (1989) One-step affinity purification of Bacillus neutral proteases using bacitracin-silica. Journal of Biochemical and Biophysical Methods 18, 209-220.
6. van den Burg, B., Eijsink, V.G.H., Stulp, B.K. and Venema, G. (1990) Identification of autodigestion target sites in Bacillus subtilus neutral protease. Biochemical Journal 18, 209-220.
7. Carson, M.J. (1987) Ribbon models for macromolecules. Journal of Molecular Graphics 5, 103-106.
8. Chakraborty, T., Ebel, F., Domann, E., Neibuhr, K., Gerstel, B., Pistor, S., Temm-Grove, C.J., Jockusch, B.M., Reinhard, M., Walter, U. and Wehland, J. (1995) A focal adhesion factor directly linking intracellularly motile Listeria monocytogenes and Listeria ivanovii to the actin-based cytoskeleton of mammalian cells. EMBO Journal 14, 1314-1321.
9. Coffey, A., Rombouts, F.M. and Abee, T. (1996) Influence of environmental parameters on phosphatidylcholine phospholipase C production in Listeria monocytogenes: a convenient method to differentiate L. monocytogenes from other Listeria species. Applied and Environmental Microbiology 62, 1252-1256.
10. Cossart, P. and Lecuit, M. (1998) Interactions of Listeria monocytogenes with mammalian cells during entry and actin-based movement: bacterial factors, cellular ligands and signaling. EMBO Journal 17, 3797-3806.
11. Dabiri, G.A., Sanger, J.M., Portnoy, D.A. and Southwick, F.S. (1990) Listeria monocytogenes moves rapidly through the host cytoplasm by inducing directional actin assembly. Procedings of the National Academy of Sciences USA 87, 6068-6072.
12. Dallmier, A.W. and Martin, S.E. (1990) Catalase, superoxide dismutase, and hemolysin and heat susceptibility of Listeria monocytogenes after growth in media containing sodium chloride. Applied and Environmental Microbiology 56, 2807-2810.
13. Domann, E., Leimeister-Wächter, M., Goebel, W. and Chakraborty, T. (1991) Molecular cloning, sequencing and identification of a metalloprotease gene from Listeria monocytogenes that is species specific and physically linked to the listeriolysin gene. Infection and Immunity 59, 65-72.
14. Eijsink, V.G.H., Veltman, O.R., Aukema, W., Vriend, G. and Venema, G. (1995) Structural determinants of the stability of thermolysin-like proteinases. Structural Biology 2, 374-379.
15. Farber, J.M. and Peterkin, P.I. (1991) Listeria monocytogenes: a food-borne pathogen. Microbiological Reviews 55, 476-511.
16. Falkow, S., Isberg, R.R. and Portnoy, D.A. (1992) The interaction of bacteria with mammalian cells. Annual Review of Cell Biology 8, 333-363.
17. Fontana, A. (1991) How nature engineers protein (thermo) stability. In: ed. Di Presco, G., Life Under Extreme Conditions: Biological Adaptation, pp. 89-113. Berlin: Springer Verlag.
18. Friederich, E., Gouin, E., Hellio, R., Kocks, C., Cossart, P. and Louvard, D. (1995) Targetting of Listeria monocytogenes ActA protein as a tool to dissect both actin-based cell morphogenesis and ActA function. EMBO Journal 14, 2731-2744.
19. Goldfine, H., Knob, C., Alford, D. and Bentz, J. (1995) Membrane permeabilization by Listeria monocytogenes phosphatidylinositol-specific phospholipase C is independent of phospholipid hydrolysis and cooperative with listeriolysin O. Proceedings of the National Academy of Sciences USA 92, 2979-2983.
20. Holland, D.R., Hausrath, A.C., Juers, D. and Matthews, B.W. (1995) Structural analysis of zinc substitutions in the active site of thermolysin. Protein Science 4, 1955-1965.
21. Holmes, M.A. and Matthews, B.W. (1982) Structure of thermolysin refined at 1.6 Å resolution. Journal of Molecular Biology 160, 623-639.
22. Holmquist, B. and Vallee, B.L. (1974) Metal substitutions and inhibition of thermolysin. Journal of Biological Chemistry 249, 4601-4607.
23. Ikemura, H. and Inouye, M. (1988) In vitro processing of prosubtilisin produced in Escherichia coli. Journal of Biological Chemistry 263, 12959-12963.
24. Ireton, K. and Cossart, P. (1997) Host-pathogen interactions during entry and actin-based movement of Listeria monocytogenes. Annual Review of Genetics 31, 113-138.
25. Kuhn, M. and Goebel, W. (1995) Molecular studies on the virulence of Listeria monocytogenes. Genetic Engineering 17, 31-51.
26. Lebrun, M., Mengaud, J., Ohayon, H., Nato, F. and Cossart, P. (1996) Internalin must be on the bacterial surface to mediate entry of Listeria monocytogenes into epithelial cells. Molecular Microbiology: 21, 579-592.
27. Leimeister-Wächter, M., Domann, E. and Chakraborty, T. (1992) The expression of virulence genes in Listeria monocytogenes is thermoregulated. Journal of Bacteriology 174, 947-952.
28. Mansfield, J., Vriend, G., Dijkstra, B.W., Venema, G., Ulbrich-Hofmann, R. and Eijsink (1995) In: Perspectives on Protein Engineering eds. Geisow, M.J. and Epton, R., pp. 205-206. Kingswinford, UK: Mayflower Worldwide Ltd.
29. Marquis, H., Bouwer, H.G.A., Hinrichs, D.J. and Portnoy, D.A. (1993) Intracytoplasmic growth and virulence of Listeria monocytogenes auxotrophic mutants. Infection and Immunity 61, 3576-3760.
30. Mengaud, J., Geoffroy, C. and Cossart, P. (1991) Identification of a new operon involved in Listeria monocytogenes virulence: its first gene encodes a protein homologous to bacterial metalloproteases. Infection and Immunity 59, 1043-1049.
31. Parida, S.K., Domann, E., Rohde, M., Muller, S., Darji, A., Hain, T., Wehland, J. and Chakraborty, T. (1998) Internalin B is essential for adhesion and mediates the invasion of Listeria monocytogenes into human endothelial cells. Molecular Microbiology 28, 81-93.
32. Piez, K. A. and Eagle, H. (1958) The free amino acid pool of cultured human cells. Journal of Biological Chemistry 231, 533-545.
33. Poyart, C., Abachin, E., Razafimanantsoa, I. and Berche, P. (1993) The zinc metalloprotease of Listeria monocytogenes is required for maturation of phosphatidylcholine phospholipase C: direct evidence obtained by gene complementation. Infection and Immunity 61, 1576-1580.
34. Premaratne, R.J., Lin, W.-J. and Johnson, E.A. (1991) Development of an improved chemically defined medium for Listeria monocytogenes. Applied and Environmental Microbiology 57, 3046-3048.
35. Raveneau, J., Geoffroy, C., Beretti, J.L., Gailard, J.L., Alouf, J. and Berche, P. (1992) Reduced virulence of a Listeria monocytogenes phospholipase C-deficient mutant obtained by transposon insertion into the zinc metalloprotease gene. Infection and Immunity 60, 916-921.
36. Roy, S.K. and Kundu, S.K. (1979) Chemically modified porous silica gel as a bioadsorbent and a biocatalyst. Analytical Biochemistry 98, 238-241.
37. Seeliger, H.P.R. and Jones, D. (1986) In: Bergey's Manual of Systematic Bacteriology, vol. 2, ed. Sneath, P.H.A., Mair, N.S., Sharpe, M.E. and Holt, J.G., pp. 2135-1245. London: Williams & Wilkins.
38. Sheehan, B., Kocks, C., Dramsi, S., Gouin, E., Klarsfeld, A.D., Mengaud, J. and Cossart, P. (1994) Molecular and genetic determinants of the Listeria monocytogenes infectious process. Current Topics in Microbiology and Immunology 192, 187-216.
39. Theriot, J.A., Mitchison, T.J., Tilney, L.G. and Portnoy, D.A. (1992) The rate of actin-based motility of intracellular Listeria monocytogenes equals the rate of actin polymerisation. Nature 357, 257-260.
40. Vazquez-Boland, J.-A., Kocks, C., Dramsi, S., Geoffroy, C., Mengaud, J. and Cossart, P. (1992) Nucleotide sequence of the lecithinase operon of Listeria monocytogenes and possible role of lecithinase in cell-to-cell spread. Infection and Immunity 60, 219-230.
41. Verheul, A., Hagting, A., Amezaga, M.-R., Booth, I.R., Rombouts, F.M. and Abee, T. (1995) A di-and tripeptide transport system can supply Listeria monocytogenes ScottA with amino acids essential for growth. Applied and Environmental Microbiology 61, 226-233.
42. Vriend, G. (1990) WHAT IF, a molecular modelling and drug design program. Journal of Molecular Graphics 8, 52-56.