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. 1989 Nov;86(22):8936-40.
doi: 10.1073/pnas.86.22.8936.

Alloreactivity studied with mutants of HLA-A2

J Santos-Aguado  1 , M A Crimmins, S J Mentzer, S J Burakoff, J L Strominger
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Alloreactivity studied with mutants of HLA-A2

J Santos-Aguado et al. Proc Natl Acad Sci U S A. 1989 Nov.

Abstract

Based on the crystal structure of HLA-A2.1 and the recognition of a panel of mutant HLA-A2.1 molecules by a large number of alloreactive cytotoxic T lymphocyte clones, a model to explain alloreactivity is described. In this model recognition of an allogeneic major histocompatibility complex molecule by a self-restricted T-cell receptor occurs as the result of accommodation by the receptor of a few amino acid differences in the major histocompatibility complex molecule--i.e., cross-recognition. Alloreactivity is the result of the presence in the foreign antigen binding site of the allogeneic major histocompatibility complex molecule of unusual self-peptides, reactivity to which could not have been eliminated by negative thymic selection.

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