Landais D, Matthes H, Benoist C, Mathis D
Proc Natl Acad Sci U S A. 1985 May;82(9):2930-4. doi: 10.1073/pnas.82.9.2930.
The murine Ia antigens, heterodimeric glycoproteins on the surface of immunocompetent cells, restrict immune recognition by their influence on cell-cell interactions. Many serological specificities have been mapped to these molecules, and monoclonal antibodies directed against some of these determinants block antigen presentation to T lymphocytes. As a step toward a better understanding of Ia function, we sought to define the molecular basis of Ia.2 and Ia.19, specificities found on the A alpha chain of only the k or of both k and r haplotypes, respectively. We report nucleotide sequences for the A alpha chain cDNAs of the k, r, and s haplotypes, which, when compared to previously published A alpha sequences, demonstrate the existence of one k-specific amino acid residue and of another present only in the k and r haplotypes. These residues must thus play an important role in the generation of Ia.2 and Ia.19 specificities.
小鼠Ia抗原是免疫活性细胞表面的异二聚体糖蛋白,通过影响细胞间相互作用来限制免疫识别。许多血清学特异性已定位到这些分子上,针对其中一些决定簇的单克隆抗体可阻断抗原呈递给T淋巴细胞。作为更好地理解Ia功能的一步,我们试图确定Ia.2和Ia.19的分子基础,这两种特异性分别仅在k单倍型或k和r单倍型的Aα链上发现。我们报告了k、r和s单倍型Aα链cDNA的核苷酸序列,与先前发表的Aα序列相比,这些序列显示存在一个k特异性氨基酸残基和另一个仅存在于k和r单倍型中的氨基酸残基。因此,这些残基必定在Ia.2和Ia.19特异性的产生中起重要作用。