ArticleBiochimica et biophysica acta2013
Comparison of the catalytic properties of the botulinum neurotoxin subtypes A1 and A5.
Article in Biochimica et biophysica acta, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed.
- Characterisation of the SNAP-25 and SNAP-23 cleavage properties of the botulinum neurotoxin-like protein from Enterococcus.Journal of neural transmission (Vienna, Austria : 1996) · 2026Article
- Cryo-EM structure of the botulinum neurotoxin A/SV2B complex and its implications for translocation.Nature communications · 2025Article
- Botulinum Neurotoxin A4 Has a 1000-Fold Reduced Potency Due to Three Single Amino Acid Alterations in the Protein Receptor Binding Domain.International journal of molecular sciences · 2023Article
- A Comprehensive Structural Analysis ofToxins · 2023Review
- Article
- Analgesic potential of different available commercial brands of botulinum neurotoxin-A in formalin-induced orofacial pain in mice.Toxicon: X · 2021Article
- Article
- High-resolution crystal structures of the botulinum neurotoxin binding domains from subtypes A5 and A6.FEBS open bio · 2020Article
- Review
- Comparative functional analysis of mice after local injection with botulinum neurotoxin A1, A2, A6, and B1 by catwalk analysis.Toxicon : official journal of the International Society on Toxinology · 2019Article
- Functional detection of botulinum neurotoxin serotypes A to F by monoclonal neoepitope-specific antibodies and suspension array technology.Scientific reports · 2019Article
- Biological Toxins as the Potential Tools for Bioterrorism.International journal of molecular sciences · 2019Review
- Why Are Botulinum Neurotoxin-Producing Bacteria So Diverse and Botulinum Neurotoxins So Toxic?Toxins · 2019Review
- Article
- Review
- Botulinum Neurotoxins: Biology, Pharmacology, and Toxicology.Pharmacological reviews · 2017Review
- In vivo onset and duration of action varies for botulinum neurotoxin A subtypes 1-5.Toxicon : official journal of the International Society on Toxinology · 2015Article
- Current status and future directions of botulinum neurotoxins for targeting pain processing.Toxins · 2015Review
- Isolation and functional characterization of the novel Clostridium botulinum neurotoxin A8 subtype.PloS one · 2015Article
- Holotoxin Activity of Botulinum Neurotoxin Subtype A4 Originating from a Nontoxigenic Clostridium botulinum Expression System.Applied and environmental microbiology · 2014Article
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8 authors.
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Abstract
Clostridium botulinum neurotoxins (BoNTs) cause the life-threatening disease botulism through the inhibition of neurotransmitter release by cleaving essential SNARE proteins. There are seven serologically distinctive types of BoNTs and many subtypes within a serotype have been identified. BoNT/A5 is a recently discovered subtype of type A botulinum neurotoxin which possesses a very high degree of sequence similarity and identity to the well-studied A1 subtype. In the present study, we examined the endopeptidase activity of these two BoNT/A subtypes and our results revealed significant differences in substrate binding and cleavage efficiency between subtype A5 and A1. Distinctive hydrolysis efficiency was observed between the two toxins during cleavage of the native substrate SNAP-25 versus a shortened peptide mimic. N-terminal truncation studies demonstrated that a key region of the SNAP-25, including the amino acid residues at 151 through 154 located in the remote binding region of the substrate, contributed to the differential catalytic properties between A1 and A5. Elevated binding affinity of the peptide substrate resulted from including these important residues and enhanced BoNT/A5's hydrolysis efficiency. In addition, mutations of these amino acid residues affect the proteolytic performance of the two toxins in different ways. This study provides a better understanding of the biological activity of these toxins, their performance characteristics in the Endopep-MS assay to detect BoNT in clinical samples and foods, and is useful for the development of peptide substrates.
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