Title: Use of Surface Plasmon Resonance to characterise binding of Botulinum Type A toxin-haemagglutinin complex to gangliosides
Authors: M.C. Blome, B.C. Yowler, R. O'Keeffe, N. Panjwani, A.M. Pickett, C-L. Schengrund
Addresses: Department of Biochemistry and Molecular Biology, The Pennsylvania State University, College of Medicine, Hershey, PA, USA. ' Department of Biology, Geneva College, Beaver Falls, PA 15010, USA. ' Ipsen Biopharm Ltd., Ash Road, Wrexham Industrial Estate, Wrexham, LL13 9UF, UK. ' Ipsen Biopharm Ltd., Ash Road, Wrexham Industrial Estate, Wrexham, LL13 9UF, UK. ' Ipsen Biopharm Ltd., Ash Road, Wrexham Industrial Estate, Wrexham, LL13 9UF, UK. ' Department of Biochemistry and Molecular Biology H171, The Pennsylvania State University College of Medicine, Hershey, PA 17033, USA
Abstract: Botulinum Type A toxin (BoNT/A)-haemagglutinin complex, marketed as Dysport®, is licensed for several clinical applications. Currently, potency is measured using the mouse lethality assay. To identify why preparations may differ, both endoprotease activity plus ability of the toxin complex to adhere to cells and be transported to where it acts must be monitored. Inhibition of any of those steps could affect efficacy. As a first step in such assessments, affinity of 9 different preparations of BoNT/A-haemagglutinin complex for ganglioside GT1b was measured using surface plasmon resonance. Similar binding affinities were obtained for all nine. [Received 4 October 2007; Accepted 12 November 2007]
Keywords: botulinum type A toxin-haemagglutinin complex; gangliosides; surface plasmon resonance; binding affinity; haemagglutinin; botulism; endoprotease activity.
The Botulinum Journal, 2008 Vol.1 No.1, pp.88 - 99
Published online: 25 Jun 2008 *Full-text access for editors Access for subscribers Purchase this article Comment on this article