From the Mouse to the Mass Spectrometer: Detection and Differentiation of the Endoproteinase Activities of Botulinum Neurotoxins A−G by Mass Spectrometry
Citations Over TimeTop 10% of 2005 papers
Abstract
We have developed an assay (Endopep-MS) that detects the specific endoproteinase activities of all seven BoNT types by mass spectrometry (MS). Each BoNT type cleaves a unique site on proteins involved in neuronal transmission. Target peptide substrates based on these proteins identify a BoNT type by its enzymatic action on the substrate and the production of two peptide products, which are then detected by matrix-assisted laser desorption/ionization time-of-flight MS or liquid chromatography electrospray ionization MS/MS. We showed the ability to detect all seven toxin types in a multiplexed assay format. The detection limits achieved range from 0.039 to 0.625 mouse LD(50)/mL for toxin types A, B, E, and F in a buffer system. The Endopep-MS assay is the first to differentiate all seven BoNT types, is sensitive, specific, and has the potential to quantify toxin activity.
Related Papers
- → Dysport®: Pharmacological properties and factors that influence toxin action(2009)59 cited
- → Occurrence of a new toxin and tetrodotoxin in two species of the gastropod mollusk Nassariidae(1992)25 cited
- → Effect of sulfhydryl group modification on the neurotoxic action of a sea snake toxin(1984)10 cited
- → Production of C2 toxin by Clostridium botulinum types C and D as determined by its vascular permeability activity(1982)15 cited
- → Clostridium botulinum type D neurotoxin: Purification and detection(1989)4 cited