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Blood, Vol. 95 No. 8 (April 15), 2000:
pp. 2617-2623
Tracing uptake of C3dg-conjugated antigen into B cells via
complement receptor type 2 (CR2, CD21)
Michael W. Hess,
Michael G. Schwendinger,
Eeva-Liisa Eskelinen,
Kristian Pfaller,
Margit Pavelka,
Manfred P. Dierich, and
Wolfgang
M. Prodinger
From the Institut für Anatomie und Histologie and the Institut
für Hygiene und Sozialmedizin, Universität Innsbruck,
Innsbruck; the Institut für Histologie und Embryologie II,
Universität Wien, Vienna, Austria; and the Institute of
Biotechnology, University of Helsinki, Helsinki, Finland.
Electron microscopy was used to study the internalization and
delivery of ligands for complement receptor type 2 (CR2, CD21) to
endocytic compartments of B-lymphoblastoid Raji cells. Opsonized antigen was mimicked with purified C3dg conjugated to colloidal gold.
C3dg-gold bound specifically to the cell surface in a time-dependent manner, and preincubation of the cells with a monoclonal antibody blocking the CR2 ligand-binding site completely inhibited any C3dg-gold
binding. Notably, the binding of C3d-gold was confined to cell surface
protrusions, eg, microvilli. C3dg-gold was apparently internalized
through coated pits located at the bases of microvilli and could be
traced to different compartments of the endocytic pathway. The
morphologic characteristics and intracellular distribution of these
multivesicular or multilaminar structures were compatible with those of
compartments known to harbor major histocompatibility complex (MHC)
class II molecules. Immunolabeling showed that the internalized
C3dg-gold colocalized with MHC class II in these structures. These data
provide the first ultrastructural evidence that complement-coated
antigens are endocytosed by antigen-nonspecific B cells by CR2 and are
delivered to the compartments in which peptide loading for antigen
presentation occurs. They support the notion that CR2 may play a role
in antigen presentation by B cells regardless of B-cell receptor specificity.
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