Structural highlights
Publication Abstract from PubMedBotulinum neurotoxins (BoNTs) are the causative agents of a potentially lethal paralytic disease targeting cholinergic nerve terminals. Multiple BoNT serotypes exist, with types A, B and E being the main cause of human botulism. Their extreme toxicity has been exploited for cosmetic and therapeutic uses to treat a wide range of neuromuscular disorders. Although naturally occurring BoNT types share a common end effect, their activity varies significantly based on the neuronal cell-surface receptors and intracellular SNARE substrates they target. These properties are the result of structural variations that have traditionally been studied using biophysical methods such as X-ray crystallography. Here, we determined the first structures of botulinum neurotoxins using single-particle cryogenic electron microscopy. The maps obtained at 3.6 and 3.7 A for BoNT/B and /E, respectively, highlight the subtle structural dynamism between domains, and of the binding domain in particular. This study demonstrates how the recent advances made in the field of single-particle electron microscopy can be applied to bacterial toxins of clinical relevance and the botulinum neurotoxin family in particular. Structural Analysis of Botulinum Neurotoxins Type B and E by Cryo-EM.,Kosenina S, Martinez-Carranza M, Davies JR, Masuyer G, Stenmark P Toxins (Basel). 2021 Dec 23;14(1). pii: toxins14010014. doi:, 10.3390/toxins14010014. PMID:35050991[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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