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Abstract
Heat shock protein (hsp)-peptide complexes are taken up by dendritic cells through hsp receptors such as CD91. Endocytosed hsp-peptide complexes are re-presented (or cross-presented) by the DCs through their MHC I (and to a lesser extent, MHC II) molecules. In an analysis of re-presentation of ovalbumin-derived SIINFEKL peptides from ova-expressing E.G7 cells, we observe that the hsp-peptide complexes and not the ova protein are the dominant form of antigen utilized in re-presentation. These observations and other considerations (to be discussed at the meeting) lead us to explore the hypothesis that hsp-peptide complexes represent a dominant instrument of cross-presentation and cross-priming in vivo.
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