Schiavo G, Santucci A, Dasgupta B R, Mehta P P, Jontes J, Benfenati F, Wilson M C, Montecucco C
Centro CNR Biomembrane, Università di Padova, Italy.
FEBS Lett. 1993 Nov 29;335(1):99-103. doi: 10.1016/0014-5793(93)80448-4.
SNAP-25, a membrane-associated protein of the nerve terminal, is specifically cleaved by botulinum neurotoxins serotypes A and E, which cause human and animal botulism by blocking neurotransmitter release at the neuromuscular junction. Here we show that these two metallo-endopeptidase toxins cleave SNAP-25 at two distinct carboxyl-terminal sites. Serotype A catalyses the hydrolysis of the Gln197-Arg198 peptide bond, while serotype E cleaves the Arg180-Ile181 peptide lineage. These results indicate that the carboxyl-terminal region of SNAP-25 plays a crucial role in the multi-protein complex that mediates vesicle docking and fusion at the nerve terminal.
SNAP-25是一种神经末梢的膜相关蛋白，可被A型和E型肉毒杆菌神经毒素特异性切割，这两种毒素通过阻断神经肌肉接头处的神经递质释放而导致人和动物肉毒中毒。我们在此表明，这两种金属内肽酶毒素在两个不同的羧基末端位点切割SNAP-25。A型催化Gln197-Arg198肽键的水解，而E型切割Arg180-Ile181肽链。这些结果表明，SNAP-25的羧基末端区域在介导神经末梢囊泡对接和融合的多蛋白复合物中起关键作用。
