Tetanus and botulism neurotoxins: a novel group of zinc-endopeptidases.
作者： Tonello F , Schiavo G , Montecucco C , Rossetto O , Morante S
DOI:
关键词: Syntaxin 、 Synaptic vesicle 、 Chemistry 、 Membrane protein 、 Biochemistry 、 Structural motif 、 Neurotoxin 、 Synaptobrevin 、 Protein subunit 、 Botulism
摘要: Tetanus and botulinum neurotoxins are produced by bacteria of the genus Clostridium cause paralytic syndromes tetanus botulism with a persistent inhibition neurotransmitter release at central peripheral synapses, respectively. These consist two disulfide-linked polypeptides: H (100 kDa) is responsible for neurospecific binding cell penetration L(50 kDa), zinc-endopeptidase specific three protein subunits neuroexocytosis apparatus. neurotoxin serotypes B, D, F, G cleave single sites, which differ each neurotoxin. VAMP/synaptobrevin, membrane synaptic vesicles. Botulinum A E SNAP-25, presynaptic membrane, different carboxyl-terminal peptide bonds. Serotype C cleaves specifically syntaxin, another nerve plasmalemma. The target specificity these metallo-proteinases relies on double recognition their substrates based interactions cleavage site non contiguous segment that contains structural motif common to VAMP, SNAP-25 syntaxin.
参考文章(10)
G. Schiavo, B. Poulain, O. Rossetto, F. Benfenati, L. Tauc, C. Montecucco, Tetanus toxin is a zinc protein and its inhibition of neurotransmitter release and protease activity depend on zinc. The EMBO Journal. ,vol. 11, pp. 3577- 3583 ,(1992) , 10.1002/J.1460-2075.1992.TB05441.X
Lawrence C. Sellin, The Action of Botulinum Toxin at the Neuromuscular Junction Medical biology. ,vol. 59, pp. 11- 20 ,(1980) , 10.21236/ADA094643
S. Yamasaki, A. Baumeister, T. Binz, J. Blasi, E. Link, F. Cornille, B. Roques, E.M. Fykse, T.C. Südhof, R. Jahn, Cleavage of members of the synaptobrevin/VAMP family by types D and F botulinal neurotoxins and tetanus toxin Journal of Biological Chemistry. ,vol. 269, pp. 12764- 12772 ,(1994) , 10.1016/S0021-9258(18)99941-2
F.X. Gomis-Rüth, L.F. Kress, W. Bode, First structure of a snake venom metalloproteinase : a prototype for matrix metalloproteinases/collagenases The EMBO Journal. ,vol. 12, pp. 4151- 4157 ,(1993) , 10.1002/J.1460-2075.1993.TB06099.X
Marie D. Anderson, Neil Fairweather, Ian G. Charles, Paul Emsley, Neil W. Isaacs, Gerry MacDermott, Crystallographic characterization of tetanus toxin fragment C. Journal of Molecular Biology. ,vol. 230, pp. 673- 674 ,(1993) , 10.1006/JMBI.1993.1181
Wolfram Bode, Franz-Xaver Gomis-Rüth, Walter Stöckler, Astacins, serralysins, snake venom 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 Letters. ,vol. 331, pp. 134- 140 ,(1993) , 10.1016/0014-5793(93)80312-I
Giampietro G. Schiavo, Fabio Benfenati, Bernard Poulain, Ornella Rossetto, Patrizia Polverino de Laureto, Bibhuti R. DasGupta, Cesare Montecucco, Tetanus and botulinum-B neurotoxins block neurotransmitter release by proteolytic cleavage of synaptobrevin Nature. ,vol. 359, pp. 832- 835 ,(1992) , 10.1038/359832A0
Clifford C. SHONE, Conrad P. QUINN, Robin WAIT, Bassam HALLIS, Sarah G. FOOKS, Peter HAMBLETON, Proteolytic cleavage of synthetic fragments of vesicle-associated membrane protein, isoform-2 by botulinum type B neurotoxin FEBS Journal. ,vol. 217, pp. 965- 971 ,(1993) , 10.1111/J.1432-1033.1993.TB18327.X
ME Schwab, K Suda, H Thoenen, Selective retrograde transsynaptic transfer of a protein, tetanus toxin, subsequent to its retrograde axonal transport. Journal of Cell Biology. ,vol. 82, pp. 798- 810 ,(1979) , 10.1083/JCB.82.3.798
G. Payling Wright, THE NEUROTOXINS OF CLOSTRIDIUM BOTULINUM AND CLOSTRIDIUM TETANI Pharmacological Reviews. ,vol. 7, pp. 413- 465 ,(1955)