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Membrane immunoglobulin functions to internalize bound antigen for its subsequent processing and presentation to T cells. Although the five immunoglobulin isotypes exhibit considerable differences in their cytoplasmic domains, we show by use of matched B lymphoma transfectants that all isotypes manifest a similar high efficacy in antigen presentation. Experiments using mutant receptors reveal that this efficacy can be ascribed to the alpha/beta sheath of the receptor, where presentation correlates with internalization of polyvalent antigen. Efficient presentation is restored to a sheathless antigen receptor by providing it with only the cytoplasmic domain of the beta sheath polypeptide. This restoration of activity does not depend on the tyrosine residues in the beta cytoplasmic tail, implying that antigen receptor-mediated presentation can occur by a pathway distinct from that used by the Fc receptor Fc gamma RIII.

Original publication

DOI

10.1016/0092-8674(93)90473-4

Type

Journal article

Journal

Cell

Publication Date

10/09/1993

Volume

74

Pages

939 - 946

Keywords

Amino Acid Sequence, Animals, B-Lymphocytes, Cell Line, Cytoplasm, Endocytosis, Immunoglobulin D, Immunoglobulin G, Immunoglobulin Isotypes, Immunoglobulin M, Kinetics, Macromolecular Substances, Mice, Mice, Inbred C57BL, Molecular Sequence Data, Plasmids, Receptors, Antigen, B-Cell, Receptors, Transferrin, Sequence Homology, Amino Acid, Transfection, Tyrosine