Alloreactivity studied with mutants of HLA-A2

J. Santos-Aguado; M. A.V. Crimmins; S. J. Mentzer; S. J. Burakoff; J. L. Strominger

doi:10.1073/pnas.86.22.8936

Alloreactivity studied with mutants of HLA-A2

J. Santos-Aguado, M. A.V. Crimmins, S. J. Mentzer, S. J. Burakoff, J. L. Strominger

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54 Scopus citations

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 accomodation 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.

Original language	English
Pages (from-to)	8936-8940
Number of pages	5
Journal	Proceedings of the National Academy of Sciences of the United States of America
Volume	86
Issue number	22
DOIs	https://doi.org/10.1073/pnas.86.22.8936
State	Published - 1989
Externally published	Yes

Keywords

allogeneic recognition
class I major histocompatibility complex molecules
cytotoxic T cells
histocompatibility

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10.1073/pnas.86.22.8936

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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 accomodation 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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AU - Santos-Aguado, J.

AU - Crimmins, M. A.V.

AU - Mentzer, S. J.

AU - Burakoff, S. J.

AU - Strominger, J. L.

PY - 1989

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AB - 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 accomodation 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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Alloreactivity studied with mutants of HLA-A2

Abstract

Keywords

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