International Immunology, Vol. 14, No. 3, 241-247,
March 2002
© 2002 Japanese Society for Immunology
Modeling the presentation of C3d-coated antigen by B lymphocytes: enhancement by CR1/2BCR co-ligation is selective for the co-ligating antigen
1 Department of Immunology, Loránd Eötvös University, Pázmány Péter s. 1/C, Budapest, Hungary
2 Research Group of the Hungarian Academy of Sciences, Budapest, Hungary
3 Center of Immunology, Bucharest, Romania
Correspondence to: A. Erdei, Department of Immunology, Loránd Eötvös University, Pázmány Péter s. 1/C, Budapest, Hungary. E-mail: anna.erdai{at}freemail.hu
We have used a set of single-chain variable fragment antibodies (sc) genetically fused with an influenza hemagglutinin-derived peptide as a means to investigate the role of CR1 and CR2 in antigen presentation by B cells. When incubated with the B cell lymphoma 2PK3, peptide-containing sc specific for either CR1 or CR1/2 mediated activation of the hemagglutinin peptide-specific T cell line IP-12-7, as assessed by IL-2 production. Efficient presentation was dependent on the binding of the constructs to CR1/2, implying that receptor-mediated endocytosis is responsible for the effect. Cross-linkage of CR1/2 or CD19 by mAb did not increase the extent of T cell activation. However, when CR1/2 was co-ligated with the BCRusing either polyclonal goat anti-mouse IgG or recombinant protein LAthe antigen concentration required to activate T cells decreased by two orders of magnitude. Moreover, this enhancement was selective for the antigen included in these complexes and did not affect the presentation of a free peptide or of antigen bound to CR1/2 excluded from the complexes. These results suggest that B cells may bind various C3d-coated antigens at a time, but only the one which reacts with the BCR will be processed with high efficiency. This mechanism may ensure the specificity of cognate T cell help.
Keywords: antigen presentation, B lymphocytes, complement
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