Heteromeric glycolipid complexes as modulators of autoantibody and lectin binding.

Glycolipids act as receptors for a wide range of antibodies, lectins and microbes. It has long been recognised that the local topography of glycolipids in the plasma membrane is critical to these recognition events, although the biological basis for this has been relatively under-investigated. Withi...

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Principais autores: Rinaldi, S, Brennan, K, Willison, H
Formato: Journal article
Idioma:English
Publicado em: 2010
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author Rinaldi, S
Brennan, K
Willison, H
author_facet Rinaldi, S
Brennan, K
Willison, H
author_sort Rinaldi, S
collection OXFORD
description Glycolipids act as receptors for a wide range of antibodies, lectins and microbes. It has long been recognised that the local topography of glycolipids in the plasma membrane is critical to these recognition events, although the biological basis for this has been relatively under-investigated. Within the last five years, emerging evidence indicates that hetero-dimeric clusters of different glycolipids can form highly distinct and specific epitopes for antibody and lectin binding. The initial observation that these ganglioside complexes (GSC) could either dramatically enhance or equally well inhibit the binding of neuropathy sera has now been reproduced for a number of other lectins, including siglecs and bacterial toxins. Here we review the initial discovery of GSC as antibody binding domains and the subsequent studies delineating their broader functional importance. Potential mechanisms underlying these effects are considered, although much remains to be investigated and explained. However, the implications for this field are potentially widespread, ranging from glycoarray design, structural biology and membrane biophysics, through to the biological consequences of glycolipid complex organisation in plasma membranes.
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spelling oxford-uuid:fa543469-053f-482c-a44c-0c13f67f73ee2022-03-27T13:04:50ZHeteromeric glycolipid complexes as modulators of autoantibody and lectin binding.Journal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:fa543469-053f-482c-a44c-0c13f67f73eeEnglishSymplectic Elements at Oxford2010Rinaldi, SBrennan, KWillison, HGlycolipids act as receptors for a wide range of antibodies, lectins and microbes. It has long been recognised that the local topography of glycolipids in the plasma membrane is critical to these recognition events, although the biological basis for this has been relatively under-investigated. Within the last five years, emerging evidence indicates that hetero-dimeric clusters of different glycolipids can form highly distinct and specific epitopes for antibody and lectin binding. The initial observation that these ganglioside complexes (GSC) could either dramatically enhance or equally well inhibit the binding of neuropathy sera has now been reproduced for a number of other lectins, including siglecs and bacterial toxins. Here we review the initial discovery of GSC as antibody binding domains and the subsequent studies delineating their broader functional importance. Potential mechanisms underlying these effects are considered, although much remains to be investigated and explained. However, the implications for this field are potentially widespread, ranging from glycoarray design, structural biology and membrane biophysics, through to the biological consequences of glycolipid complex organisation in plasma membranes.
spellingShingle Rinaldi, S
Brennan, K
Willison, H
Heteromeric glycolipid complexes as modulators of autoantibody and lectin binding.
title Heteromeric glycolipid complexes as modulators of autoantibody and lectin binding.
title_full Heteromeric glycolipid complexes as modulators of autoantibody and lectin binding.
title_fullStr Heteromeric glycolipid complexes as modulators of autoantibody and lectin binding.
title_full_unstemmed Heteromeric glycolipid complexes as modulators of autoantibody and lectin binding.
title_short Heteromeric glycolipid complexes as modulators of autoantibody and lectin binding.
title_sort heteromeric glycolipid complexes as modulators of autoantibody and lectin binding
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AT brennank heteromericglycolipidcomplexesasmodulatorsofautoantibodyandlectinbinding
AT willisonh heteromericglycolipidcomplexesasmodulatorsofautoantibodyandlectinbinding