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Increased mobility of major histocompatibility complex I-peptide complexes decreases the sensitivity of antigen recognition.

The Journal of biological chemistry (2008-06-27)
Jean-Manuel Segura, Philippe Guillaume, Silke Mark, Danijel Dojcinovic, Alexandre Johannsen, Giovanna Bosshard, Georgi Angelov, Daniel F Legler, Horst Vogel, Immanuel F Luescher
ABSTRACT

CD8(+) cytotoxic T lymphocytes (CTL) can recognize and kill target cells expressing only a few cognate major histocompatibility complex (MHC) I-peptide complexes. This high sensitivity requires efficient scanning of a vast number of highly diverse MHC I-peptide complexes by the T cell receptor in the contact site of transient conjugates formed mainly by nonspecific interactions of ICAM-1 and LFA-1. Tracking of single H-2K(d) molecules loaded with fluorescent peptides on target cells and nascent conjugates with CTL showed dynamic transitions between states of free diffusion and immobility. The immobilizations were explained by association of MHC I-peptide complexes with ICAM-1 and strongly increased their local concentration in cell adhesion sites and hence their scanning by T cell receptor. In nascent immunological synapses cognate complexes became immobile, whereas noncognate ones diffused out again. Interfering with this mobility modulation-based concentration and sorting of MHC I-peptide complexes strongly impaired the sensitivity of antigen recognition by CTL, demonstrating that it constitutes a new basic aspect of antigen presentation by MHC I molecules.

MATERIALS
Product Number
Brand
Product Description

Sigma-Aldrich
Atto 647, BioReagent, suitable for fluorescence, ≥90% (HPCE)
Sigma-Aldrich
Atto 647 NHS ester, BioReagent, suitable for fluorescence, ≥80% (coupling to amines)
Sigma-Aldrich
Atto 647 maleimide, BioReagent, suitable for fluorescence, ≥90% (coupling to thiols)

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