TY - JOUR
T1 - Qa-2, H-2K, and H-2D alloantigens evolved from a common ancestral gene
AU - Soloski, M. J.
AU - Uhr, J. W.
AU - Flaherty, L.
AU - Vitetta, E. S.
PY - 1981
Y1 - 1981
N2 - The Tla region located on the murine 17th chromosome controls several serologically defined cell surface antigens. These antigens, referred to as Qa-1-5 and TL, are expressed on a variety of hematopoeitic cell populations. In the present studies we have immunoprecipitated isotopically labeled Qa-2 and H-2 molecules from mitogen-stimulated B6 spleen cells. Sequential immunoprecipitation experiments have shown that the determinants recognized by αQa-2, αH-2K6, and αH-2D6 alloantisera reside on separate molecular species. Comparative mapping of the arginine-labeled tryptic peptides from Qa-2, H-2K6, and H-2D6 molecules indicate that Qa-2 is structurally distinct but that there is considerable structual homology; 21-43% of the Qa-2 peptides co-chromatograph with peptides derived from H-2Db and H-2Kb, respectively. Similar levels of homology are observed when Qa-2 is compared with H-2K(k) or H-2D(d). The results show that the Qa-2 alloantigen is encoded by a locus separate from the loci encoding H-2K or H-2D alloantigens, but that the Qa-2, H-2K, and H-2D alloantigens are sufficiently related at the primary structural level to indicate that they evolved from a common primordial gene.
AB - The Tla region located on the murine 17th chromosome controls several serologically defined cell surface antigens. These antigens, referred to as Qa-1-5 and TL, are expressed on a variety of hematopoeitic cell populations. In the present studies we have immunoprecipitated isotopically labeled Qa-2 and H-2 molecules from mitogen-stimulated B6 spleen cells. Sequential immunoprecipitation experiments have shown that the determinants recognized by αQa-2, αH-2K6, and αH-2D6 alloantisera reside on separate molecular species. Comparative mapping of the arginine-labeled tryptic peptides from Qa-2, H-2K6, and H-2D6 molecules indicate that Qa-2 is structurally distinct but that there is considerable structual homology; 21-43% of the Qa-2 peptides co-chromatograph with peptides derived from H-2Db and H-2Kb, respectively. Similar levels of homology are observed when Qa-2 is compared with H-2K(k) or H-2D(d). The results show that the Qa-2 alloantigen is encoded by a locus separate from the loci encoding H-2K or H-2D alloantigens, but that the Qa-2, H-2K, and H-2D alloantigens are sufficiently related at the primary structural level to indicate that they evolved from a common primordial gene.
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U2 - 10.1084/jem.153.5.1080
DO - 10.1084/jem.153.5.1080
M3 - Article
C2 - 6788884
AN - SCOPUS:0019404997
SN - 0022-1007
VL - 153
SP - 1080
EP - 1093
JO - Journal of Experimental Medicine
JF - Journal of Experimental Medicine
IS - 5
ER -