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Requirements for a Self Antigen Recognition in Humans
* Laboratory of Experimental Immunology, Instituto di Ricovero e Cura a Carattere Scientifico Salvatore Maugeri Foundation, and
Biotechnology Research Laboratory, Instituto di Ricovero e Cura a Carattere Scientifico Policlinico San Matteo, Pavia, Italy;
Department of Clinical and Biological Sciences, University of Turin, Orbassano, Italy; and
European Institute of Oncology, Milan, Italy
TCR-
and -
chains are composed of somatically rearranged V,
D, and J germline-encoded gene segments that confer Ag specificity.
Recent crystallographic analyses revealed that TCR- has more
contacts with peptide than TCR-, suggesting the possibility that
peptide recognition predominantly relies on TCR-. T cells specific
for the self Ag Melan-A/MART-1 possess an exceptionally high precursor
frequency in human histocompatibility leukocyte Ag-A2 individuals. This
provided a unique situation for assessment of the structural
relationship between TCR and peptide/MHC ligand at both the pre- and
postimmune levels. Molecular and phenotypic analysis of many different
Melan-A-specific T cell populations revealed that a structural
constraint is imposed on the TCR for engagement with Melan-A peptides
presented by HLA-A2, namely the highly preferential use of a particular
TCRAV segment, AV2. Examination of CD8 single-positive thymocytes
indicated that this preferential use in forming the Melan-A-specific
TCR is mainly imposed by intrathymic positive selection. Our data
demonstrate a dominant function of TCRAV2 segment in forming the TCR
repertoire specific for the human self Ag Melan-A/MART-1 and support
the view that Ag recognition is mediated predominantly by
TCR-.
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