C. Seitz et al., THE MONOCLONAL-ANTIBODY HCA2 RECOGNIZES A BROADLY SHARED EPITOPE ON SELECTED CLASSICAL AS WELL AS SEVERAL NONCLASSICAL HLA CLASS-I MOLECULES, Molecular immunology, 35(13), 1998, pp. 819-827
HCA2 is a widely used monoclonal antibody. thought to be highly select
ive for HLA-A and -G heavy chains. We demonstrate here that it also sh
ows affinity to HLA-B73 and HLA-E molecules on intact cells. By compar
ing the differences in the amino acid (AA) sequences of several HLA cl
ass I alleles that are either recognised or not recognised by HCA2, a
likely epitope of HCA2 has been deduced. It extends from position 76 t
o position 83 of the alpha(1)-domain. In intact cells, the solvent-exp
osed AA in positions 76 (Ala, Val or Met), 80 (Asn or Thr) and 83 (Gly
) are likely to constitute the recognition region. Inhibition experime
nts with peptides spanning the region of the alpha(1)-domain from posi
tion 74 to 85 of various HLA class I heavy chains prove that HCA2 reco
gnizes a broadly shared epitope on HLA-E, -F and -G molecules as well
as selected HLA-A, -B and -C antigens. (C) 1998 Elsevier Science Ltd.
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