Picture of Open Access badges

Discover Open Access research at Strathprints

It's International Open Access Week, 24-30 October 2016. This year's theme is "Open in Action" and is all about taking meaningful steps towards opening up research and scholarship. The Strathprints institutional repository is a digital archive of University of Strathclyde research outputs. Explore recent world leading Open Access research content by University of Strathclyde researchers and see how Strathclyde researchers are committing to putting "Open in Action".


Image: h_pampel, CC-BY

Anti-GQ1b ganglioside antibodies mediate complement-dependent destruction of the motor nerve terminal

O'Hanlon, G.M. and Plomp, J.J. and Chakrabarti, M. and Morrison, I. and Wagner, E.R. and Goodyear, C.S. and Yin, X. and Trapp, B.D. and Conner, J. and Molenaar, P.C. and Stewart, S. and Rowan, E.G. and Willison, H.J. (2001) Anti-GQ1b ganglioside antibodies mediate complement-dependent destruction of the motor nerve terminal. Brain, 124 (5). pp. 893-906. ISSN 0006-8950

Full text not available in this repository. (Request a copy from the Strathclyde author)


Miller-Fisher syndrome is an autoimmune neuropathy characterized by ataxia, areflexia and ophthalmoplegia, and in the majority of cases the presence of high titres of anti-GQ1b ganglioside antibodies. In an ex vivo model, human and mouse anti-GQ1b antibodies have been shown previously to induce a complement-dependent {alpha}-latrotoxin-like effect on the murine motor endplate, i.e. they bring about massive quantal release of acetylcholine and eventually block neuromuscular transmission. Using immunofluorescence microscopy with image analysis, we show here that the late stages of this electrophysiological effect temporally coincide with the loss of heavy neurofilament (200 kDa) and type III ß-tubulin immunostaining and structural breakdown of the nerve terminal, as demonstrated by electron microscopy. Ultrastructurally, axon terminals were disorganized, depleted of vesicles, and subdivided by the infiltrating processes of capping Schwann cells. These findings provide clear pathological evidence to support a role for anti-ganglioside antibodies in mediating nerve terminal injury and further advance the view that this site may be of importance as a target in some human neuropathies.