Alloreactivity studied with mutants of HLA-A2

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

Research output: Contribution to journalArticlepeer-review

54 Scopus citations


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 languageEnglish
Pages (from-to)8936-8940
Number of pages5
JournalProceedings of the National Academy of Sciences of the United States of America
Issue number22
StatePublished - 1989
Externally publishedYes


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


Dive into the research topics of 'Alloreactivity studied with mutants of HLA-A2'. Together they form a unique fingerprint.

Cite this