Peptide Binding to Active Class II MHC Protein on the Cell Surface

Solution studies have demonstrated the existence of two functionally distinct isomers of empty class II MHC: an active isomer that binds peptide and an inactive isomer that does not. Empty MHC molecules on the surface of APCs can load antigenic peptides directly from the extracellular medium, facili...

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Veröffentlicht in:The Journal of immunology (1950) 2001-06, Vol.166 (11), p.6680-6685
Hauptverfasser: Vacchino, Judith F, McConnell, Harden M
Format: Artikel
Sprache:eng
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Zusammenfassung:Solution studies have demonstrated the existence of two functionally distinct isomers of empty class II MHC: an active isomer that binds peptide and an inactive isomer that does not. Empty MHC molecules on the surface of APCs can load antigenic peptides directly from the extracellular medium, facilitating the generation of a diverse peptide repertoire for T cell presentation. In this report, we examine I-Ek on the surface of Chinese hamster ovary cells with respect to the active and inactive isomers. As in the case of purified soluble active I-Ek, active I-Ek on the cell surface is unstable, decaying to the inactive form in approximately 14 min. Evidence is presented suggesting that at steady state
ISSN:0022-1767
1550-6606
DOI:10.4049/jimmunol.166.11.6680