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Primary structural studies of the Qa-2 alloantigen: implications for the evolution of the MHC

Nature volume 296, pages 759761 (22 April 1982) | Download Citation

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Abstract

The murine major histocompatibility complex (MHC) contains a number of loci encoding cell-surface glycoproteins of molecular weight (MW) 40,000–45,000 which are non-covalently associated with β2-microglobulin. The products of this large multigene family, collectively referred to as class I gene products, include H–2K,-D,-L and -R, which are encoded by the H–2 complex, and Qa-1, -2 and TL, encoded by the Tla region telomeric to H–2 (refs 1–5). Functional studies have shown that the H–2K, -D and -L gene products serve as important self-recognition structures in immune responses6,7; a functional role for the other class I gene products has not been established. Tryptic peptide map comparisons and primary sequence analyses have indicated that H–2K, -D and -L are 70–85% homologous with respect to their amino acid sequences8–10. The data, however, have failed to reveal structural features unique to gene products of a given locus. Recent tryptic peptide map comparisons of the Tla gene products, Qa-2 and TL, have shown that Qa-2, H-2K and -D are more closely related to each other than to TL11,12. Here we present the NH2-terminal sequence of the Qa-2 alloantigen. Our results, together with those of previous studies, show that Qa-2 has significant homology to H–2 antigens but differs in that Qa-2 molecules lack extensive polymorphism and the Qa-2 heavy chain has two additional NH2-terminal amino acids and several critical amino acid interchanges compared with H–2 antigens.

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Author information

Affiliations

  1. Department of Microbiology, University of Texas Health Science Center, Dallas, Texas 75235, USA

    • Mark J. Soloski
    • , Jonathan W. Uhr
    •  & Ellen S. Vitetta

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https://doi.org/10.1038/296759a0

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