QA-2 MOLECULES ARE PEPTIDE RECEPTORS OF HIGHER STRINGENCY THAN ORDINARY CLASS-I MOLECULES

QA-2 MOLECULES ARE PEPTIDE RECEPTORS OF HIGHER STRINGENCY THAN ORDINARY CLASS-I MOLECULES
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DOI:
10.1038/361642a0
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发表时间:
1993-02-18
期刊:
影响因子:
64.8
通讯作者:
RAMMENSEE, HG
RAMMENSEE, HG
中科院分区:
综合性期刊1区
文献类型:
--
作者:
ROTZSCHKE, O;FALK, K;RAMMENSEE, HG

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主要组织相容性复合体(MHC)的I类分子将肽运输到细胞表面,以供T细胞监测。配体特异性要求严格,并且在不同等位基因之间存在差异。在此我们报道对“非经典的”糖磷脂酰肌醇锚定的小鼠I类分子Qa - 2的天然配体的分析。这些分子的功能尚不清楚;它们可作为“非限制性”细胞毒性T细胞的识别结构,但尚未发现其向T细胞呈递肽,尽管其DNA序列表明其具有与“经典的”I类分子相似的肽结合槽,并且在少数情况下其他非经典的I类分子能够呈递抗原。对天然Qa - 2配体的混合测序表明,Qa - 2分子确实是肽受体,其配体特异性与经典的I类分子相似,即主要的肽长度为9个氨基酸,具有锚定位点以及肽的疏水性末端。但是其配体特异性比其他I类分子更为严格:在9个位置中,2个是锚定位点,并且4个位置的占有率相当有限。
CLASS I molecules of the major histocompatibility complex (MHC) transport peptides to the cell surface for surveillance by T cells1. Ligand specificity is stringent and differs from allele to allele2-4. Here we report analysis of natural ligands of 'unconventional' glycophosphatidyl-anchored mouse class I molecules, Qa-2. The function of these molecules is unclear5,6; they can serve as recognition structures for 'unrestricted' cytotoxic T cells but have not been found to present peptides to T cells, although the DNA sequence suggests a similar peptide binding groove to that of 'conventional' class I molecules7, and other unconventional class I molecules can present antigens in a few cases8-10. Pool sequencing of natural Qa-2 ligands shows that Qa-2 molecules are indeed peptide receptors, having ligand specificity similar to that of conventional class I molecules, that is, a predominant length of nine amino acids, anchor positions, and hydrophobic termination of peptides. But ligand specificity is much more stringent than with other class I molecules: of the nine positions, two are anchors and four have rather limited occupancy.