Warren Edus H, Vigneron Nathalie J, Gavin Marc A, Coulie Pierre G, Stroobant Vincent, Dalet Alexandre, Tykodi Scott S, Xuereb Suzanne M, Mito Jeffrey K, Riddell Stanley R, Van den Eynde Benoît J
Program in Immunology, Clinical Research Division, Fred Hutchinson Cancer Research Center, Seattle, WA 98109, USA.
Science. 2006 Sep 8;313(5792):1444-7. doi: 10.1126/science.1130660.
CD8-positive T lymphocytes recognize peptides that are usually derived from the degradation of cellular proteins and are presented by class I molecules of the major histocompatibility complex. Here we describe a human minor histocompatibility antigen created by a polymorphism in the SP110 nuclear phosphoprotein gene. The antigenic peptide comprises two noncontiguous SP110 peptide segments spliced together in reverse order to that in which they occur in the predicted SP110 protein. The antigenic peptide could be produced in vitro by incubation of precursor peptides with highly purified 20S proteasomes. Cutting and splicing probably occur within the proteasome by transpeptidation.
CD8 阳性 T 淋巴细胞识别通常源自细胞蛋白降解且由主要组织相容性复合体 I 类分子呈递的肽段。在此,我们描述了一种由 SP110 核磷蛋白基因多态性产生的人类次要组织相容性抗原。该抗原肽由两个不连续的 SP110 肽段组成,它们以与预测的 SP110 蛋白中出现的顺序相反的顺序拼接在一起。通过将前体肽与高度纯化的 20S 蛋白酶体一起孵育,可在体外产生该抗原肽。切割和拼接可能通过转肽作用在蛋白酶体内发生。