Bacterial toxins with intracellular protease activity

Clinica Chimica Acta

Volumn 291, Issue 2, 2000, Pages 189-199

  Rossetto, Ornella ^a   De Bernard,, Marina ^a   Pellizzari, Rossella ^a   Vitale, Gaetano ^a   Caccin, Paola ^a   Schiavo, Giampietro ^a   Montecucco, Cesare ^a  

^a UNIVERSITY OF PADOVA   (Italy)

Author keywords

Clostridial neurotoxins; Lethal factor of Bacillus anthracis; Metallo proteases; Vacuolating cytotoxin of Helicobacter pylori

Indexed keywords

BACTERIAL TOXIN; BOTULINUM TOXIN; NEUROTOXIN; PROTEINASE; SYNAPTOSOMAL ASSOCIATED PROTEIN 25;

BACILLUS ANTHRACIS; ENZYME ACTIVITY; ENZYME ANALYSIS; ENZYME SPECIFICITY; HELICOBACTER PYLORI; LETHAL GENE; NONHUMAN; PRIORITY JOURNAL; PROTEIN DOMAIN; REVIEW; SEQUENCE ANALYSIS;

ANTHRAX; BACILLUS ANTHRACIS; BACTERIA (MICROORGANISMS); HELICOBACTER PYLORI;

EID: 0034651823     PISSN: 00098981     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0009-8981(99)00228-4     Document Type: Article

References (62)

1. Menestrina G., Schiavo G., Montecucco C. Molecular mechanisms of action of bacterial protein toxins. Mol. Aspects Med. 15:1994;79-193.
2. Montecucco C., Papini E., Schiavo G. Bacterial protein toxins penetrate cells via a four-step mechanism. FEBS Lett. 346:1994;92-98.
3. Simpson L.L., Botulinum neurotoxins and tetanus toxin. 1989;Academic Press, New York.
4. Montecucco C., Schiavo G. Structure and function of botulinum neurotoxins. Q Rev Biophys. 28:1995;423-472.
5. Rothman J.E. Mechanism of intracellular protein transport. Nature. 372:1994;55-63.
6. Südhof T.C. The synaptic vesicle cycle: a cascade of protein-protein interactions. Nature. 375:1995;645-653.
7. Schiavo G., Benfenati F., Poulain B., et al. Tetanus and botulinum-B neurotoxins block neurotransmitter release by a proteolytic cleavage of synaptobrevin. Nature. 359:1992;832-835.
8. Schiavo G., Shone C.C., Rossetto O., Alexandre F.C.G., Montecucco C. Botulinum neurotoxin serotype F is a zinc endopeptidase specific for VAMP/synaptobrevin. J Biol Chem. 268:1993;11516-11519.
9. Schiavo G., Rossetto O., Catsicas S., et al. Identification of the nerve terminal targets of botulinum neurotoxin serotypes A, D and E. J Biol Chem. 268:1993;23784-23787.
10. Yamasaki S., Baumeister A., Binz T., et al. Cleavage of members of the synaptobrevin/VAMP family by types D and F botulinal neurotoxins and tetanus toxin. J Biol Chem. 269:1994;12764-12772.
11. Schiavo G., Malizio C., Trimble W.S., et al. Botulinum G neurotoxin cleaves VAMP/synaptobrevin at a single Ala-Ala peptide bond. J Biol Chem. 269:1994;20213-20216.
12. Schiavo G., Santucci A., DasGupta B.R., et al. Botulinum neurotoxins serotypes A and E cleave SNAP-25 at distinct COOH-terminal peptide bonds. FEBS Lett. 335:1993;99-103.
13. Binz T., Blasi J., Yamasaki S. Proteolysis of SNAP-25 by types E and A botulinal neurotoxins. J Biol Chem. 269:1994;1617-1620.
14. Blasi J., Chapman E.R., Yamasaki S., Binz T., Niemann H., Jahn R. Botulinum neurotoxin C blocks neurotransmitter release by means of cleaving HPC-1/syntaxin. EMBO J. 12:1993;4821-4828.
15. Schiavo G., Shone C.C., Bennett M.K., Scheller R.H., Montecucco C. Botulinum neurotoxin type C cleaves a single Lys-Ala bond within the carboxil terminal region of syntaxin. J Biol Chem. 270:1995;10566-10570.
16. Williamson L.C., Halpern J.L., Montecucco C., Brown E., Neale E.A. Clostridial neurotoxins and substrate proteolysis in intact neurons: botulinum neurotoxin C acts on synaptosomal-associated protein of 25 kDa. J Biol Chem. 271:1996;7694-7699.
17. Osen-Sand A., Staple J.K., Naldi E., et al. Common and distinct fusion proteins in axonal growth and transmitter release. J Comp Neurol. 367:1996;222-234.
18. Foran P., Lawrence G.W., Shone C.C., Foster K.A., Dolly J.O. Botulinum neurotoxin C1 cleaves both syntaxin and SNAP-25 in intact and permeabilized chromaffin cells: correlation with its blockade of catecholamine release. Biochemistry. 35:1996;2630-2636.
19. Jankovic J., Hallett M., Therapy with botulinum toxin. 1994;Marcel Dekker, New York.
20. Eleopra R., Tugnoli V., Rossetto O., Montecucco C., De Grandis D. Botulinum neurotoxin serotype C: a novel effective botulinum toxin therapy in human. Neurosci Lett. 224:1997;91-94.
21. Leppla S.H. Alouf J.E., Freer J.H., Sourcebook of bacterial protein toxins. 1991;277-302 Academic Press, London.
22. Leppla S.H., Moss J., Iglewski B., Vaughan M., Tu A.T. Handbook of natural toxins. vol. 8:1995;543-572 Marcel Dekker, New York.
23. Hanna P.C., Collier R. Rappuoli R., Montecucco C., Protein toxins and their use in cell biology. 1997;91-93 Oxford University Press, Oxford.
24. Pezard C., Berche P., Mock M. Contribution of individual toxin components to virulence of Bacillus anthracis. Infect Immun. 59:1991;3472-3477.
25. Gordon V.M., Leppla S.H., Hewlett E L. Inhibitors of receptor-mediated endocytosis block the entry of Bacillus anthracis adenylate cyclase toxin but not that of Bordetella pertussis adenylate cyclase toxin. Infect Immun. 56:1988;1066-1069.
26. Milne J.C., Furlong D., Hanna P.C., Wall J.S., Collier R.J. Anthrax protective antigen forms oligomers during intoxication of mammalian cells. J Biol Chem. 269:1994;20607-20612.
27. Singh Y., Leppla S.H., Bhatnagar R., Friedlander A.M. Internalization and processing of B. anthracis lethal toxin by toxin-sensitive and -resistant cells. J Biol Chem. 264:1989;11099-11102.
28. Petosa C., Collier R.J., Klimpel K.R., Leppla S.H., Liddington R.C. Crystal structure of the protective antigen. Nature. 385:1997;833-838.
29. Leppla S.H. Anthrax toxin edema factor: a bacterial adenylate cyclase that increases cyclic AMP concentrations of eukaryotic cells. Proc Natl Acad Sci USA. 79:1982;3162-3166.
30. Bragg T.S., Robertson D.L. Nucleotide sequence and analysis of the lethal factor gene (lef) from Bacillus anthracis. Gene. 81:1989;45-54.
31. Klimpel K.R., Arora N., Leppla S.H. Anthrax toxin lethal factor contains a Zn metalloprotease consensus sequence which is required for lethal toxin activity. Mol Microbiol. 13:1994;1093-1100.
32. Kochi S.K., Schiavo G., Mock M., Montecucco C. Zinc content of the Bacillus anthracis lethal factor. FEMS Microbiol Lett. 124:1994;343-348.
33. Ezzell J.W., Ivins B.E., Leppla S.H. Immunoelectrophoretic analysis, toxicity, and kinetics of in vitro production of the protective antigen and lethal factor components of Bacillus anthracis toxin. Infect Immun. 45:1984;761-767.
34. Friedlander A.M. Macrophages are sensitive to anthrax lethal toxin through an acid-dependent process. J Biol Chem. 261:1986;7123-7126.
35. Hanna P.C., Kochi S., Collier R.J. Biochemical and physiological changes induced by anthrax lethal toxin in J774 macrophage-like cells. Mol Biol Cell. 3:1992;1269-1277.
36. Hanna P.C., Acosta D., Collier R.J. On the role of macrophages in anthrax. Proc Natl Acad Sci USA. 90:1993;10198-10201.
37. Hanna P.C., Kruskal B.A., Ezekowitz R.A.B., Bloom B.R., Collier R.J. Role of macrophage oxidative burst in the action of anthrax lethal toxin. Mol Med. 1:1994;7-18.
38. Schiavo G., Rossetto O., Santucci A., DasGupta B.R., Montecucco C. Botulinum neurotoxins are zinc proteins. J Biol Chem. 267:1992;23479-23483.
39. Montecucco C., Schiavo G. Structure and function of tetanus and botulinum neurotoxin. Q Rev Biophys. 28:1995;423-472.
40. Isaacson P.G. Gastric lymphoma and Helicobacter pylori. N Engl J Med. 330:1994;1310-1311.
41. Correa P. Helicobacter pylori and gastric carcinogenesis. Am J Surg Pathol. 19:1995;37-43.
42. Parsonnet J. Helicobacter pylori: the size of the problem. Gut. 43:(suppl 1):1998;S6-9.
43. Leunk R.D., Johnson P.T., David B.C., Kraft W.G., Morgan D.R. Cytotoxin activity in broth-culture filtrates of Campylobacter pylori. J Med Microbiol. 26:1988;93-99.
44. Cover T.L., Blaser M.J. Purification and characterization of the vacuolating toxin from Helicobacter pylori. J Biol Chem. 287:1992;10570-10575.
45. Cover T.L. The vacuolating cytotoxin of Helicobacter pylori. Mol Microbiol. 20:1997;241-246.
46. Telford J.L., Ghiara P., Dell'Orco M., et al. Purification and characterization of the vacuolating toxin from Helicobacter pylori. J Exp Med. 179:1994;1653-1658.
47. Lupetti P., Heuser J.E., Manetti R., et al. Oligomeric and subunit structure of the Helicobacter pylori vacuolating cytotoxin. J Cell Biol. 133:1996;801-807.
48. Moll G., Papini E., Colonna R., et al. Lipid interaction of the 37 kDa and 58 kDa fragments of the Helicobacter pylori cytotoxin. Eur J Biochem. 234:1996;947-952.
49. Cover T.L., Hanson P.I., Heuser J.E. Acid-induced dissociation of VacA, the Helicobacter pylori vacuolating cytotoxin, reveals its pattern of assembly. J Cell Biol. 138:1997;759-769.
50. de Bernard M., Papini E., De Filippis E., et al. Low pH activates the vacuolating toxin of Helicobacter pylori which becomes acid and pepsin resistant. J Biol Chem. 270:1995;23937-23940.
51. Papini E., Bugnoli M., de Bernard M., Figura N., Rappuoli R., Montecucco C. Bafilomycin A1 inhibits Helicobacter pylori induced vacuolization of HeLa cells. Mol Microbiol. 7:1993;323-327.
52. Papini E., de Bernard M., Milia E., et al. Cellular vacuoles induced by Helicobacter pylori originate from late endosomal compartments. Proc Natl Acad Sci USA. 91:1994;9720-9724.
53. Nuoffer C., Balch W.E. GTPases: multifunctional molecular switches regulating vesicular traffic. Annu Rev Biochem. 63:1994;949-990.
54. Simons K., Zerial M. Rab proteins and the road maps for intracellular transport. Neuron. 11:1993;789-799.
55. Zerial M., Huber L. Guidebook to the small GTPases. 1996;Oxford University Press, Oxford.
56. Papini E., Satin B., Bucci C., et al. The small GTP binding protein rab7 is essential for cellular vacuolation induced by Helicobacter pylori cytotoxin. EMBO J. 16:1997;15-24.
57. Satin B., Norais N., Telford J.L., et al. Effect of Helicobacter pylori vacuolating toxin on maturation and extracellular release of procathepsin D and epidermal growth factor degradation. J Biol Chem. 272:1997;25022-25028.
58. Molinari M., Salio M., Galli C., et al. Selective inhibition of Ii-dependent antigen presentation by Helicobacter pylori toxin VacA. J Exp Med. 187:1998;135-140.
59. Tombola F., Carlesso C., Szabò I., et al. Helicobacter pylori vacuolating toxin forms anion-selective channels in planar lipid bilayers: possible implications for the mechanism of cellular vacuolation. Biophys J. 76:1999;1401-1409.
60. de Bernard M., Aricò B., Papini E., Telford J.L., Rappuoli R., Montecucco C. Helicobacter pylori toxin VacA induces vacuole formation by acting in the cell cytosol. Mol Microbiol. 26:1997;665-674.
61. Montecucco C., Papini E., Schiavo G. Bacterial protein toxins penetrate cells via a four-step mechanism. FEBS Lett. 346:1994;92-98.
62. de Bernard M., Burroni D., Papini E., Rappuoli R., Telford J.L., Montecucco C. Identification of the Helicobacter pylori VacA toxin domain active in the cell cytosol. Infect Immun. 66:1998;6014-6016.