Murakami S, Yokomizo H, Matsushita S, Ogawa M, Nishimura Y
Department of Neuroscience and Immunology, Kumamoto University Graduate School of Medical Sciences, Japan.
Immunol Lett. 1996 Mar;49(3):149-53. doi: 10.1016/0165-2478(96)02495-9.
We investigated binding of p53- and Ras-derived peptides with frequently observed missense mutations, to various L cell transfectants expressing a single species of HLA-DR complex, and found that: (i) all the synthetic peptides bound to various DR complexes with a variable affinity; (ii) some DR allelic products had a high affinity for both p53- and Ras-derived peptides (e.g., DRB11502), whereas others almost no affinity (e.g., DRB11101); and (iii) DR-binding motifs described in the literature can explain some of the allele-specific interactions between mutated peptides and DR complexes. Therefore, some mutated Ras- and p53-derived peptides could be tumor-specific antigens recognized by CD4+ T cells in an HLA-DR allele-specific manner.
我们研究了携带常见错义突变的p53和Ras衍生肽与表达单一HLA-DR复合物的各种L细胞转染子的结合情况，结果发现：（i）所有合成肽均以可变亲和力与各种DR复合物结合；（ii）一些DR等位基因产物对p53和Ras衍生肽均具有高亲和力（例如DRB11502），而其他一些则几乎没有亲和力（例如DRB11101）；（iii）文献中描述的DR结合基序可以解释一些突变肽与DR复合物之间的等位基因特异性相互作用。因此，一些突变的Ras和p53衍生肽可能是以HLA-DR等位基因特异性方式被CD4+ T细胞识别的肿瘤特异性抗原。
