Corinne Moulon

TL;DR: Recent developments in the analysis of the structural basis of hapten recognition, particularly by T lymphocytes, are reviewed, finding that T cells detect haptens as structural entities attached covalently or by complexation to self-peptides anchored in binding grooves of major histocompatibility antigens (MHC-proteins).

TL;DR: It is indicated that for Cu and Pd, these co‐reactivities observed in vivo in human patients might be due to cross‐reactivity at the clonal level, and the findings suggest that this is not the case for cobalt allergy, which might result from co‐sensitization of the patient to cobalt in addition to nickel.

TL;DR: Data indicate that labile, nonactivating complexes between the SE9 TCR and most HLA-DR/peptide conjugates might supply sterically optimized coordination sites for Ni ions, three of which were identified in this study.

TL;DR: It is shown that Ni-saturated HSA complexes (HSA-Ni) induce and activate Ni-specific human T cells as potently as Ni salt solutions when present at equimolar concentrations classically used for in vitro T cell stimulation.

TL;DR: A general model for Ni2+ recognition is proposed in which βHis81 and two amino acids from the NH2-terminal part of the MHC bound peptide coordinate Ni2+, which then interacts with some portion of the Vα CDR1 or CDR2 region.