The clinical eVects of botulinum toxin have been recognised since the end of the 19th century. It is the most potent neurotoxin known and it is produced by the gram negative anaerobic bacterium Clostridium botulinum. The paralytic eVect of the toxin is due to blockade of neuromuscular transmission. Injection into a muscle causes chemodenervation and local paralysis and this eVect has led to the...

The clinical eVects of botulinum toxin have been recognised since the end of the 19th century. It is the most potent neurotoxin known and it is produced by the gram negative anaerobic bacterium Clostridium botulinum. The paralytic eVect of the toxin is due to blockade of neuromuscular transmission. Injection into a muscle causes chemodenervation and local paralysis and this eVect has led to the...

This review presents a brief account of the most significant biological effects and clinical applications of botulinum neurotoxins, in a way comprehensive even for casual readers who are not familiar with the subject. The most toxic known substances in botulinum neurotoxins are polypeptides naturally synthesized by bacteria of the genus Clostridium. These polypeptides inhibit acetylcholine rele...

An analysis of SNAP-25 isoform sequences indicates that there is a highly conserved arginine residue (198 in vertebrates, 206 in the genus Drosophila) within the C-terminal region, which is cleaved by botulinum neurotoxin A, with consequent blockade of neuroexocytosis. The possibility that it may play an important role in the function of the neuroexocytosis machinery was tested at neuromuscular...

Plastic Surgery, the number of aesthetic procedures involving botulinum neurotoxin type A (BoNT-A) increased 3681% between 1997 and 2008. Almost 2.5 million procedures were performed using this neurotoxin last year, accounting for approximately 25% of all nonsurgical aesthetic procedures performed in 2008.1 Both aesthetic and therapeutic uses of this neurotoxin are likely to increase in the com...

Clostridium Botulinum Type E neurotoxin heavy chain consists of two domains: the translocation domain asthe N-terminal half and the binding domain as the Cterminal half (Hc). One effective way to neutralize botulinum neurotoxin is to inhibit binding of this toxin to neuromuscular synapses with antibodies against binding domain. Two synthetic genes, coding for Hc (the full length binding d...

Botulinal neurotoxin continues to be a concern in food safety. The molecular biology of botulinal neurotoxin gene expression in Clostridium botuli-num is poorly understood. In this study, the transcriptional and translational kinetics of expression of type A botulinal neurotoxin by C. botulinum type A strains Hall A, 62A, and NCTC 2916 were determined during 96 hours of growth. Strains were gro...

The protein receptor for Clostridium botulinum type B neurotoxin was purified 340-fold from rat synaptosomes by successive chromatography on DEAE-Sepharose, phenyl-Toyopearl, and heparin-Toyopearl columns. 125I-Labeled neurotoxin bound to lipid vesicles containing the protein receptor and ganglioside GT1b or GD1a. The reconstituted receptor showed the same affinities as the native receptor on s...

A significant number of genome sequences of Clostridium botulinum and related species have now been determined. In silico analysis of these data revealed the presence of two distinct agr loci (agr-1 and agr-2) in all group I strains, each encoding putative proteins with similarity to AgrB and AgrD of the well-studied Staphylococcus aureus agr quorum sensing system. In S. aureus, a small diffusi...

Botulinum neurotoxins have a very high affinity and specificity for their target cells requiring two different co-receptors located on the neuronal cell surface. Different toxin serotypes have different protein receptors; yet, most share a common ganglioside co-receptor, GT1b. We determined the crystal structure of the botulinum neurotoxin serotype A binding domain (residues 873-1297) alone and...