The DOI matches its Crossref record; 97 of the 97 references it cites were found in a registry or an index.
Botulinum Neurotoxin: A Marvel of Protein Design
Abstract
Botulinum neurotoxin (BoNT), the causative agent of botulism, is acknowledged to be the most poisonous protein known. BoNT proteases disable synaptic vesicle exocytosis by cleaving their cytosolic SNARE (soluble NSF attachment protein receptor) substrates. BoNT is a modular nanomachine: an N-terminal Zn 2+-metalloprotease, which cleaves the SNAREs; a central helical protein-conducting channel, which chaperones the protease across endosomes; and a C-terminal receptor-binding module, consisting of two subdomains that determine target specificity by binding to a ganglioside and a protein receptor on the cell surface and triggering endocytosis. For BoNT, functional complexity emerges from its modular design and the tight interplay between its component modules—a partnership with consequences that surpass the simple sum of the individual component's action. BoNTs exploit this design at each step of the intoxication process, thereby achieving an exquisite toxicity. This review summarizes current knowledge on the structure of individual modules and presents mechanistic insights into how this protein machine evolved to this level of sophistication. Understanding the design principles underpinning the function of such a dynamic modular protein remains a challenging task.
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1 retracted
Cocrystal structure of synaptobrevin-II bound to botulinum neurotoxin type B at 2.0 A resolution.
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SNAREpins: Minimal Machinery for Membrane Fusion
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BackgroundMolecular anatomy of a trafficking organelle
Takamori, S., Holt, M., Stenius, K., Lemke, E. A., Grønborg, M., Riedel, D., Urlaub, H., Schenck, S., Brügger, B., Ringler, P., et al. (2006) · Cell · doi:10.1016/j.cell.2006.10.030 · Cited by 2,373
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Cited by
Botulinum Neurotoxins: Biology, Pharmacology, and Toxicology
Pirazzini, M., Rossetto, O., Eleopra, R., & Montecucco, C. (2017) · Pharmacological Reviews · doi:10.1124/pr.116.012658 · Cited by 768
Agis-Torres, A., Sollhuber, M., Fernandez, M., & Sanchez-Montero, J. M. (2014) · Current Neuropharmacology · doi:10.2174/1570159x113116660047 · Cited by 202
Matheoud, D., Moradin, N., Bellemare-Pelletier, A., Shio, M. T., Hong, W. J., Olivier, M., Gagnon, É., Desjardins, M., & Descoteaux, A. (2013) · Cell Host & Microbe · doi:10.1016/j.chom.2013.06.003 · Cited by 148
Dendritic SNAREs add a new twist to the old neuron theory
Ovsepian, S. V., & Dolly, J. O. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1017235108 · Cited by 50
Hikima, T., Lee, C. R., Witkovsky, P., Chesler, J., Ichtchenko, K., & Rice, M. E. (2021) · Cell Reports · doi:10.1016/j.celrep.2021.108951 · Cited by 49
Metadata
- Authors
- Montal, M.
- Venue
- Annual Review of Biochemistry
- Publisher
- Annual Reviews
- Published
- 2010-06-07
- Volume
- 79
- Issue
- 1
- Pages
- 591-617
- ISSN
- 0066-4154 (ISSN-L)
- 1545-4509
- OpenAlex
- W2160463128
- Cited by
- 411
- References
- 97
- FWCI
- 3.68
- Type
- journal article
- Language
- en
- Open access
- closed
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