Tetanus and botulism neurotoxins: A novel group of zinc-endopeptidases

Advances in Experimental Medicine and Biology

Volumn 389, Issue , 1996, Pages 251-260

  Tonello, F ^a   Morante, S ^b   Rossetto, O ^a   Schiavo, G ^a   Montecucco, C ^a  

^a UNIVERSITY OF PADOVA   (Italy)

^b UNIVERSITY OF ROME TOR VERGATA   (Italy)

Author keywords

[No Author keywords available]

Indexed keywords

CLOSTRIDIUM; CLOSTRIDIUM BOTULINUM;

NEUROTOXIN; PROTEINASE; BOTULINUM TOXIN; METALLOPROTEINASE; NERVE PROTEIN; TETANUS TOXIN;

BOTULISM; CATALYSIS; CLOSTRIDIUM BOTULINUM; CONFERENCE PAPER; ENZYME SPECIFICITY; EXOCYTOSIS; NEUROTRANSMISSION; PRIORITY JOURNAL; PROTEIN DEGRADATION; SEROTYPING; TETANUS; AMINO ACID SEQUENCE; CHEMISTRY; METABOLISM; MOLECULAR GENETICS; REVIEW; SEQUENCE HOMOLOGY;

AMINO ACID SEQUENCE; BOTULINUM TOXINS; METALLOENDOPEPTIDASES; MOLECULAR SEQUENCE DATA; NERVE TISSUE PROTEINS; SEQUENCE HOMOLOGY, AMINO ACID; SUBSTRATE SPECIFICITY; TETANUS TOXIN;

EID: 0030330348     PISSN: 00652598     EISSN: None     Source Type: Book Series    
DOI: 10.1007/978-1-4613-0335-0_32     Document Type: Article

References (47)

1. Anderson, M.D., Fairweather. N., Charles, I.G., Emsley, P., Isaacs, N,W, and MacDermott, G. 1993, Crystallographic characterization of tetanus toxin fragment C. J. Mol. Biol., 230, 673-674.
2. Baumann, U., Wu, S., Flaherty. K.M. and McKay. D.B. 1993, Three-dimensional structure of the alkaline protease of Pseudomonas aeruginosa: a two domain protein with a calcium binding parallel beta roll motif. EMBO J., 12, 3357-3364.
3. Bennett, M.K., Calakos, N. and Scheller, R.H. 1992, Syntaxin: a synaptic protein implicated in docking of synaptic vesicles at presynaptic active zones. Science, 257, 255-259.
4. Binz, T., Blasi, J., Yamasaki, S., Baumeister, A., Link, E., Sudhof, T.C., Jahn, R. and Niemann, H. 1994, Proteolysis of SNAP-25 by types E and A botulinal neurotoxins. J. Biol. Chem., 269, 1617-1620.
5. Blasi, J., Chapman, E.R., Yamasaki, S., Binz, T., Niemann, H. and Jahn, R. 1993. Botulinum neurotoxin C blocks neurotransmitter release by means of cleaving HPC-1/syntaxin. EMBO J., 12, 4821-4828.
6. Bode, W., Gomis-Ruth, F.X., Huber, R., Zwilling, R. and Stcker, W. 1992, Structure of astacin and implication of astacins and zinc-ligation of collagenases. Nature, 358, 164-166.
7. Bode, W., Gomis-Ruth, F.X. and Stcker, W. 1993, Astacins, serralysin, snake venoms and matrix metalloproteinases exhibit identical zinc-binding environments (HEXXHXXGXXH and Met-turn) and topologies and should be grouped into a common family, the "metzincins". FEBS Lett., 331, 134-140.
8. Burgen, A.S.V., Dickens, F. and Zatman, L.Y. 1949, The action of botulinum toxin on the neuromuscular junction. J. Physiol. (London), 109, 10-24.
9. DasGupta, B.R. 1989, The structure of botulinum neurotoxin. In Botulinum neurotoxins and tetanus toxin (ed L.L. Simpson), Academic Press, New York, pp. 53-67.
10. de Paiva, A., Poulain, B., Lawrence, G.W., Shone, C.C., Taue, L. and Dolly, J.O. 1993. A role for the interchain disulfide or its participating thiols in the internalization of botulinum neurotoxin A revealed by a toxin derivative that binds to ecto-acceptors and inhibits transmitter release intracellularly. J. Biol. Chem., 268, 20838-20844.
11. Gomis-Ruth, F.X., Kress, L.F. and Bode, W. 1993, First structure of a snake venom metalloproteinase: a prototype for matrix metalloproteinases/collagenases. EMBO J., 12, 4151-4157.
12. Höhne-Zell, B., Stecher, B. and Gratzl, M. 1993, Functional characterization of the catalytic site of the tetanus toxin light chain using permeabilized adrenal chromaffin cells. FEBS Lett., 336, 175-180.
13. Krieglstein, K., Henschen, A., Weller, U. and Habermann, E. 1991, Limited proteolysis of tetanus toxin: relation to activity and identification of cleavage sites. Eur. J. Biochem., 202, 41-51.
14. Jankovic, J. and Hallett, M. 1994, (eds.) Therapy with botulinum toxin. Marcel Dekker, New York.
15. Jiang, W. and Bond, J.S. 1992, Families of metalloendopeptidases and their relationships. FEBS Lett., 312, 110-114.
16. Lovejoy, B., Cleasby, A., Hassell, A.M., Longley, K., Luther, M.A., Weigl, D., McGeehan, G., McElroy, A.B., Drewry, D., Lambert M.H. and Jordan, S.R. 1994, Structure of the catalytic domain of fibroblast collagenase complexed with an inhibitor. Science, 263, 375-377.
17. Matthews, B.W., Jansonius, J.N. and Colman, P.M. 1972, Three-dimensional structure of thermolysin. Nature New. Biol., 238, 37-41.
18. Miles, E.W. 1977, Modification of histidyl residues in proteins by diethylcarbonate. Methods Enzymol., 47, 431-442.
19. Montecucco, C. and Schiavo, G. 1993, Tetanus and botulism neurotoxins: a new group of zinc proteases. Trends Biochem. Sci. 18, 324-327.
20. Montecucco, C. and Schiavo, G. 1994, Mechanism of action of tetanus and botulism neurotoxins. Mol. Microbiol. 13, 1-8.
21. Montecucco, C., Papini, E. and Schiavo, G. 1994, Ba cterial protein toxins penetrate cells via a four-step mechanism. FEBS Lett. 346, 92-98.
22. Niemann, H. 1991, Molecular biology of clostridial neurotoxins. In A Sourcebook of Bacterial Protein Toxins (eds J.E. Alouf and J.H. Freer), Academic Press, London, pp. 303-348.
23. Osen-Sand, A., Catsicas, M., Staple, J.K., Jones, K.A., Ayala, G., Knowles, J., Grenningloh, G. and Catsicas, S. 1993, Inhibition of axonal growth by SNAP-25 antisense oligonucleotides in vitro and in vivo. Nature, 364, 445-448.
24. Oyler, G.A., Higgins, G.A., Hart, R.A., Battenberg, E., Billingsley, M., Bloom, F.E. and Wilson, M.C. 1989, The identification of a novel synaptosomal-associated protein, SNAP-25, differently expressed by neuronal subpopulations. J. Cell. Biol. 109, 3039-3052.
25. Pauptit, R.A., Karlsson, R., Picot, D., Jenkins, J.A., Niklaus-Reimer, A.S. and Jansonius, J.N. 1988, Crystal structure of neutral protease from Bacillus cereus refined at 3.0 A resolution and comparison with the homologous but more thermostable enzyme thermolysin. J. Mol. Biol., 199, 525-537.
26. Payling-Wright, G. 1955, The neurotoxins of Clostridium botulinum and Clostridum tetani. Pharmacol. Rev., 7, 413-465.
27. Ramon, G. and Descombey, P.A. 1925, Sur l'immunization antitetanique et sur la production de l'antitoxine tetanique. Compt. Rend. Soc. Biol., 93, 508-598.
28. Schiavo, G., Papini, E., Genna, G. and Montecucco, C. 1990, An intact interchain disulfide bond is required for the neurotoxicity of tetanus toxin. Infect. Immun., 58, 4136-4141.
29. Schiavo, G., Poulain, B., Rossetto, O., Benfenati, F., Tauc, L. and Montecucco, C. 1992a. Tetanus toxin is a zinc protein and its inhibition of neurotrasmitter release and protease activity depend on zinc. EMBO J., 11, 3577-3583.
30. Schiavo, G., Benfenati, F., Poulain, B., Rossetto, O., Polverino de Laureto, P., DasGupta, B.R. and Montecucco, C. 1992b, Tetanus and botulinum-B neurotoxins block neurotransmitter release by a proteolytic cleavage of synaptobrevin. Nature, 359, 832-835.
31. Schiavo, G., Rossetto, O., Santucci, A., DasGupta, B.R. and Montecucco, C. 1992c, Botulinum neurotoxins are zinc proteins. J. Biol. Chem., 267, 23479-23483.
32. Schiavo, G., Shone, C.C., Rossetto, O., Alexandre, F.C.G. and Montecucco, C. 1993a, Botulinum neurotoxin serotype F is a zinc endopeptidase specific for VAMP synaptobrevin. J. Biol. Chem., 268, 11516-11519.
33. Schiavo, G., Rossetto, O., Catsicas, S., Polverino de Laureto, P., DasGupta, B.R., Benfenati, F. and Montecucco, C. 1993b, Identification of the nerve-terminal targets of botulinum neurotoxins serotypes A, D and E. J. Biol. Chem., 268, 23784-23787.
34. Schiavo, G., Santucci, A., DasGupta, B.R., Metha, P.P., Jontes, J., Benfenati, F., Wilson, M.C. and Montecucco, C. 1993c, Botulinum neurotoxins serotypes A and E cleave SNAP-25 at distinct COOH-terminal peptide bonds. FEBS Lett., 335, 99-103.
35. Schiavo, G., Malizio, C., Trimble, W.S., Polverino de Laureto, P., Milan, G., Sugiyama, H., Johnson, E.A. and Montecucco, C. 1994a, Botulinum G neurotoxin cleaves VAMP/synaptobrevin at a single Ala-Ala peptide bond. J. Biol. Chem. 269, 20213-20216.
36. Schiavo, G., Rossetto, O. and Montecucco, C. 1994b, in "Zinc metalloproteases in Health and Disease", Hooper, N.M. Editor, Ellis Horwood, London, in press.
37. Schwab, M.E., Suda, K. and Thoenen, H. 1979, Selective retrograde trans-synaptic transfer of a protein, tetanus toxin, subsequent to its retrograde axonal transport. J. Cell. Biol., 82, 798-810.
38. Simpson, L.L. 1989, (ed) Botulinum neurotoxins and tetanus toxin. Academic Press, New York.
39. Shone, C.C., Quinn, C.P., Wait, R., Hallis, B., Fooks, S.G. and Hambleton, P. 1993, Proteolytic cleavage of synthetic fragments of vesicle-associated membrane protein, isoform-2 by botulinum type B neurotoxin. Eur. J. Biochem. 217, 965-971.
40. Stevens, R.C., Evenson, M.L., Tepp, W. and DasGupta, B.R. 1991, Crystallization and preliminary X-ray analysis of botulinum neurotoxin type A. J. Mol. Biol. 222, 877-880.
41. Thayer, M.M., Flaherty, K.M. and McKay, D.B. 1991, Three-dimensional structure of the elastase of Pseudomonas aeruginosa at 1.5 A resolution. J. Biol. Chem., 266, 2864-2871.
42. Trimble, W.S., Cowan, D.M. and Scheller, R.H. 1988, VAMP-1: a synaptic vesicle-associated integral membrane protein. Proc. Natl. Acad. Sci. USA, 85, 4538-4542.
43. Vallee, B.L. and Auld, D.S. 1990, Zinc coordination, function and structure of zinc enzymes and other proteins. Biochemistry. 29, 5647-5659.
44. Van Heyningcn, W.E. (1968) Tetanus. Sci. Am., 218, 69-77.
45. Yamasaki, S., Hu, Y., Binz, T., Kalkuhl, A., Kurazono, H., Tamura, T., Jahn, R., Kandel, E. & Niemann, H. 1994a, Synaptobrevin/VAMP of Aplisia californica: structure and proteolysis by tetanus and botulinal neurotoxins type D and F. Proc. Natl. Acad. Sci. USA, 91, 4688-4692.
46. Yamasaki, S., Baumeister, A., Binz, T., Blasi, J., Link, E., Cornille, F., Roques, B., Fykse, EM., Südhof, TC., Jahn, R., Niemann, H., 1994b, Cleavage of members of the synaptobrevin/VAMP family by types D and F botulinal neurotoxins and tetanus toxin. J. Biol. Chem., 269, 12764-12772.
47. Wellhoner, H.H. 1992, Tetanus and botulinum neurotoxins. In Handbook of Experimental Pharmacology, vol. 102 (eds H. Herken and F. Hucho), Springer-Verlag, Berlin, pp. 357-417.