Radcliffe, Catherine M., Arnold, James N., Suter, David M., Wormald, Mark R., Harvey, David J., Royle, Louise, Mimura, Yusuke, Kimura, Yoshinobu, Sim, Robert B., Inogès, Susana, Rodriguez-Calvillo, Mercedes, Zabalegui, Natalia, de Cerio, Ascensión López-Díaz, Potter, Kathleeen N., Mockridge, C. Ian, Dwek, Raymond A., Bendandi, Maurizio, Rudd, Pauline M. and Stevenson, Freda K.
Human follicular lymphoma cells contain oligomannose glycans in the antigen-binding site of the B-cell receptor
The Journal of Biological Chemistry, 282, (10), . (doi:10.1074/jbc.M602690200).
Full text not available from this repository.
Expression of surface immunoglobulin appears critical for the growth and survival of B-cell lymphomas. In follicular lymphoma, we found previously that the Ig variable (V) regions in the B-cell receptor express a strikingly high incidence of N-glycosylation sequons, NX(S/T). These potential glycosylation sites are introduced by somatic mutation and are lymphoma-specific, pointing to their involvement in tumor pathogenesis. Analysis of the V region sugars from lymphoma-derived IgG/IgM reveals that they are mostly oligomannose and, remarkably, are located in the antigen-binding site, possibly precluding conventional antigen binding. The Fc region contains complex glycans, confirming that the normal glycan processing pathway is intact. Binding studies indicate that the oligomannose glycans occupying the V regions are accessible to mannose-binding lectin. These findings suggest a potential contribution to lymphoma pathogenesis involving antigen-independent interaction of surface immunoglobulin of the B-cell receptor with mannose-binding molecules of innate immunity in the germinal center.
|Digital Object Identifier (DOI):
||variable region, indicate, surface, pathogenesis, receptor, surface-immunoglobulin, molecules, survival, c-type lectins, follicular lymphoma, dendritic cells, antigen, time, b-cell receptor, mutation, expression, region, involvement, lymphoma, burkitts-lymphoma, pathway, tumor, b-cell lymphoma, rheumatoid-arthritis, growth, fab fragment, immune-system, glycosylation sites, somatic mutation, binding, n-linked oligosaccharides, immunity, cells, innate, cell, immunoglobulin, b cell, b-cell-receptor, sites
|9 March 2007||Published|
||12 Sep 2008
||16 Apr 2017 17:28
|Further Information:||Google Scholar|
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