Human follicular lymphoma cells contain oligomannose glycans in the antigen-binding site of the B-cell receptor.
J Biol Chem
; 282(10): 7405-15, 2007 Mar 09.
Article
in En
| MEDLINE
| ID: mdl-17197448
ABSTRACT
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.
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Collection:
01-internacional
Database:
MEDLINE
Main subject:
Oligosaccharides
/
Receptors, Antigen, B-Cell
/
Lymphoma, Follicular
Type of study:
Etiology_studies
Limits:
Humans
Language:
En
Journal:
J Biol Chem
Year:
2007
Document type:
Article
Affiliation country: