Botulinum G neurotoxin cleaves VAMP/synaptobrevin at a single Ala-Ala peptide bond.
Similarly to other serotypes, botulinum neurotoxin serotype G (BoNT/G) contains the zinc binding motif of zinc endopeptidases. Highly purified preparations of BoNT/G show a zinc-dependent protease activity specific for VAMP/synaptobrevin, a membrane protein of synaptic vesicles. The two neuronal VAMP isoforms are cleaved with similar rates at one Ala-Ala peptide bond present in the same region, out of the several such peptide bonds present in their sequences. This site of cleavage is unique among the eight clostridial neurotoxins. VAMP proteolysis is displayed only after reduction of the single interchain disulfide bond present in the toxin, and it is inhibited by EDTA, o-phenanthroline and captopril.
Schiavo
G
G
Centro Consiglio Nazionale delle Ricerche Biomembrane, Università di Padova, Italy.
Malizio
C
C
Trimble
W S
WS
Polverino de Laureto
P
P
Milan
G
G
Sugiyama
H
H
Johnson
E A
EA
Montecucco
C
C
D000409:Alanine / Q000378:metabolism*; D000595:Amino Acid Sequence; D000818:Animals; D006868:Hydrolysis; D008565:Membrane Proteins / Q000378:metabolism*; D008969:Molecular Sequence Data; D009419:Nerve Tissue Proteins / Q000378:metabolism*; D010455:Peptides / Q000378:metabolism*; D050683:R-SNARE Proteins; D051381:Rats; D014121:Toxoids / Q000494:pharmacology*
C035415:Clostridium botulinum toxoid; D008565:Membrane Proteins; D009419:Nerve Tissue Proteins; D010455:Peptides; D050683:R-SNARE Proteins; D014121:Toxoids; D000409:Alanine