CD8 expression allows T cell signaling by monomeric peptide-MHC complexes
Physiologically, TCR signaling is unlikely to result from the cross-linking of TCR-CD3 complexes, given the low density of specific peptide-MHC complexes on antigen-presenting cells. We therefore have tested directly an alternative model for antigen recognition. We show that monomers of soluble pept...
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Veröffentlicht in: | Immunity (Cambridge, Mass.) Mass.), 1998-10, Vol.9 (4), p.467-473 |
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Format: | Artikel |
Sprache: | eng |
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Zusammenfassung: | Physiologically, TCR signaling is unlikely to result from the cross-linking of TCR-CD3 complexes, given the low density of specific peptide-MHC complexes on antigen-presenting cells. We therefore have tested directly an alternative model for antigen recognition. We show that monomers of soluble peptide-MHC trigger Ca2+ responses in CD8alphabeta+ T cells. This response is not observed in CD8- T cells and when either the CD8:MHC or CD8:Lck interactions are prevented. This demonstrates that an intact CD8 coreceptor is necessary for effective TCR signaling in response to monomeric peptide-MHC molecules. We propose that this heterodimerization of TCR and CD8 by peptide-MHC corresponds to the physiological event normally involved during antigen-specific signal transduction. |
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ISSN: | 1074-7613 |
DOI: | 10.1016/S1074-7613(00)80630-5 |