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Association of botulinum neurotoxins with synaptic vesicle protein complexes Baldwin MR; Barbieri JTToxicon 2009[Oct]; 54 (5): 570-4Botulinum neurotoxins (BoNTs) elicit flaccid paralysis by cleaving SNARE proteins within peripheral neurons. BoNTs are classified into seven serotypes, termed A-G, based on antibody cross-neutralization. Clostridia produce BoNTs as single-chain toxins that are cleaved into a di-chain protein that comprises an N-terminal zinc metalloprotease domain that is linked by a disulfide bond to the C-terminal translocation/receptor-binding domain. BoNT/A and BoNT/B utilize synaptic vesicle protein 2 (SV2) and synaptotagmin, respectively, as receptors for entry into neurons. Using affinity chromatography, BoNT/A and BoNT/B were found to bind a synaptic vesicle protein complex in CHAPS extracts of synaptic vesicles. Mass spectroscopy identified synaptic vesicle protein 2, synaptotagmin I, synaptophysin, vesicle-associated membrane protein 2, and the vacuolar ATPase-proton pump as components of the BoNT-synaptic vesicle protein complex. BoNT/A and BoNT/B possessed unique density-gradient profiles when bound to synaptic vesicle protein complexes. The identification of BoNT/A and BoNT/B bound to synaptic vesicle protein complexes provides insight into the interactions of BoNT and neuronal receptors.|Animals[MESH]|Botulinum Toxins/*metabolism/pharmacology[MESH]|Humans[MESH]|Membrane Glycoproteins/drug effects/*metabolism[MESH]|Nerve Tissue Proteins/drug effects/*metabolism[MESH]|Neurotoxins/*metabolism/pharmacology[MESH]|Protein Binding[MESH]|SNARE Proteins/drug effects/metabolism[MESH]|Structure-Activity Relationship[MESH]|Synaptic Vesicles/drug effects/*metabolism[MESH] |
