Pellizzari R, Mason S, Shone C C, Montecucco C
Centro CNR Biomembrane, Dipartimento di Scienze Biomediche, Università di Padova, Italy.
FEBS Lett. 1997 Jun 16;409(3):339-42. doi: 10.1016/s0014-5793(97)00482-1.
Botulinum neurotoxins type D and F are zinc-endopeptidases with a unique specificity for VAMP/synaptobrevin, an essential component of the exocytosis apparatus. VAMP contains two copies of a nine residue motif, termed V1 and V2, which are determinants of the interaction with tetanus and botulinum B and G neurotoxins. Here, we show that V1 plays a major role in VAMP recognition by botulinum neurotoxins D and F and that V2 is also involved in F binding. Site-directed mutagenesis of V1 and V2 indicates that different residues are the determinants of the VAMP interaction with the two endopeptidases. The study of the VAMP-neurotoxins interaction suggest a pairing of the V1 and V2 segments.
D型和F型肉毒杆菌神经毒素是锌内肽酶，对VAMP/突触囊泡蛋白（胞吐装置的必需成分）具有独特的特异性。VAMP包含两个九残基基序拷贝，称为V1和V2，它们是与破伤风以及B型和G型肉毒杆菌神经毒素相互作用的决定因素。在此，我们表明V1在D型和F型肉毒杆菌神经毒素识别VAMP中起主要作用，并且V2也参与F的结合。V1和V2的定点诱变表明，不同的残基是VAMP与这两种内肽酶相互作用的决定因素。对VAMP-神经毒素相互作用的研究表明V1和V2片段存在配对。
