Characterization of a diagnostic Fab fragment binding trimeric Lewis X

de Geus, Daniël C. and van Roon, Anne-Marie M. and Thomassen, Ellen A. J. and Hokke, Cornelis H. and Deelder, André M. and Abrahams, Jan Pieter. (2009) Characterization of a diagnostic Fab fragment binding trimeric Lewis X. Proteins: Structure, Function, and Bioinformatics , 76 (2). pp. 439-447.

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Lewis X trisaccharides normally function as essential cell-cell interaction mediators. However, oligomers of Lewis X trisaccharides expressed by the parasite Schistosoma mansoni seem to be related to its evasion of the immune response of its human host. Here we show that monoclonal antibody 54-5C10-A, which is used to diagnose schistosomiasis in humans, interacts with oligomers of at least three Lewis X trisaccharides, but not with monomeric Lewis X. We describe the sequence and the 2.5 angstrom crystal structure of its Fab fragment and infer a possible mode of binding of the polymeric Lewis X from docking studies. Our studies indicate a radically different mode of binding compared to Fab 291-2G3-A, which is specific for monomeric Lewis X, thus providing a structural explanation of the diagnostic success of 54-5C10-A.
Faculties and Departments:05 Faculty of Science > Departement Biozentrum > Structural Biology & Biophysics > Nano-diffraction of Biological Specimen (Abrahams)
UniBasel Contributors:Abrahams, Jan Pieter
Item Type:Article, refereed
Article Subtype:Research Article
Note:Publication type according to Uni Basel Research Database: Journal article
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Last Modified:05 Nov 2020 16:10
Deposited On:05 Nov 2020 16:10

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