THE INTERACTION OF SYNAPTIC VESICLE-ASSOCIATED MEMBRANE-PROTEIN SYNAPTOBREVIN WITH BOTULINUM NEUROTOXIN-D AND NEUROTOXIN-F

Botulinum neurotoxins type D and F are zinc-endopeptidases with a uniq ue specificity for VAMP/synaptobrevin, an essential component of the e xocytosis apparatus. VAMP contains two copies of a nine residue motif, termed V1 and V2, which are determinants of the interaction with teta nus and botulinum B and G neurotoxins, Here, we show that V1 plays a m ajor role in VAMP recognition by botulinum neurotoxins D and F and tha t V2 is also involved in F binding, Site-directed mutagenesis of V1 an d V2 indicates that different residues are the determinants of the VAM P interaction with the two endopeptidases. The study of the VAMP-neuro toxins interaction suggest a pairing of the V1 and V2 segments. (C) 19 97 Federation of European Biochemical Societies.