Premium
The interaction of synaptic vesicle‐associated membrane protein/synaptobrevin with botulinum neurotoxins D and F
Author(s) -
Pellizzari Rossella,
Mason Silvia,
Shone Clifford C.,
Montecucco Cesare
Publication year - 1997
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(97)00482-1
Subject(s) - synaptobrevin , synaptic vesicle , exocytosis , biochemistry , neurotoxin , chemistry , biology , vesicle , membrane
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.