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J. Exp. Med.,
Volume 187, Number 4, February 16, 1998 505-515
By
From the * Institut National de la Santé et de la Recherche Médicale, Contrat Jeune Formation
95-01, Institut Curie, Section Recherche, 75005, Paris, France; and T cell receptors on CD4+ lymphocytes recognize antigen-derived peptides presented by major
histocompatibility complex (MHC) class II molecules. A very limited set of peptides among
those that may potentially bind MHC class II is actually presented to T lymphocytes. We here
examine the role of two receptors mediating antigen internalization by antigen presenting cells,
type IIb2 and type III receptors for IgG (Fc Biologie moléculaire de gène,
Institut National de la Santé et de la Recherche Médicale U277, Institut Pasteur, 75015, Paris,
France; and § Laboratoire d'immunologie des pathologies infectieuses et tumorales, Institut Cochin
Génétique Moléculaire, Institut National de la Santé et de la Recherche Médicale U445, 75014, Paris, France
RIIb2 and FcRIII, respectively), in the selection
of peptides for presentation to T lymphocytes. B lymphoma cells expressing recombinant
FcRIIb2 or FcRIII were used to assess the presentation of several epitopes from two different antigens. 4 out of the 11 epitopes tested were efficiently presented after antigen internalization through FcRIIb2 and FcRIII. In contrast, the 7 other epitopes were efficiently presented only when antigens were internalized through FcRIII, but not through FcRIIb2.
The capacity to present these latter epitopes was transferred to a tail-less FcRIIb2 by addition
of the FcRIII-associated chain cytoplasmic tail. Mutation of a single leucine residue at position 35 of the chain cytoplasmic tail resulted in the selective loss of presentation of these
epitopes. Therefore, the nature of the receptor that mediates internalization determines the selection of epitopes presented to T lymphocytes within single protein antigens.
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