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本文引用的文献

1
Structural bases for the affinity-driven selection of a public TCR against a dominant human cytomegalovirus epitope.针对主要人类巨细胞病毒表位的公共T细胞受体亲和力驱动选择的结构基础
J Immunol. 2009 Jul 1;183(1):430-7. doi: 10.4049/jimmunol.0900556.
2
The shaping of T cell receptor recognition by self-tolerance.自身耐受性对T细胞受体识别的塑造。
Immunity. 2009 Feb 20;30(2):193-203. doi: 10.1016/j.immuni.2008.11.011. Epub 2009 Jan 22.
3
Natural micropolymorphism in human leukocyte antigens provides a basis for genetic control of antigen recognition.人类白细胞抗原中的自然微多态性为抗原识别的遗传控制提供了基础。
J Exp Med. 2009 Jan 16;206(1):209-19. doi: 10.1084/jem.20082136. Epub 2009 Jan 12.
4
Crystal structures of high affinity human T-cell receptors bound to peptide major histocompatibility complex reveal native diagonal binding geometry.与肽-主要组织相容性复合体结合的高亲和力人类T细胞受体的晶体结构揭示了天然对角结合几何结构。
Protein Eng Des Sel. 2007 Aug;20(8):397-403. doi: 10.1093/protein/gzm033. Epub 2007 Jul 20.
5
A T cell receptor flattens a bulged antigenic peptide presented by a major histocompatibility complex class I molecule.T细胞受体使主要组织相容性复合体I类分子呈递的凸起抗原肽变平。
Nat Immunol. 2007 Mar;8(3):268-76. doi: 10.1038/ni1432. Epub 2007 Jan 28.
6
Directed evolution of human T cell receptor CDR2 residues by phage display dramatically enhances affinity for cognate peptide-MHC without increasing apparent cross-reactivity.通过噬菌体展示对人T细胞受体CDR2残基进行定向进化，可显著增强对同源肽-主要组织相容性复合体的亲和力，而不会增加明显的交叉反应性。
Protein Sci. 2006 Apr;15(4):710-21. doi: 10.1110/ps.051936406.
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Selection of T cell clones expressing high-affinity public TCRs within Human cytomegalovirus-specific CD8 T cell responses.在人巨细胞病毒特异性CD8 T细胞应答中选择表达高亲和力公共TCR的T细胞克隆。
J Immunol. 2005 Nov 1;175(9):6123-32. doi: 10.4049/jimmunol.175.9.6123.
8
Stable, soluble T-cell receptor molecules for crystallization and therapeutics.用于结晶和治疗的稳定、可溶的T细胞受体分子。
Protein Eng. 2003 Sep;16(9):707-11. doi: 10.1093/protein/gzg087.
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A structural basis for immunodominant human T cell receptor recognition.免疫显性人T细胞受体识别的结构基础。
Nat Immunol. 2003 Jul;4(7):657-63. doi: 10.1038/ni942. Epub 2003 Jun 8.
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Latency and reactivation of human cytomegalovirus.人巨细胞病毒的潜伏与再激活
J Infect. 2002 Feb;44(2):73-7. doi: 10.1053/jinf.2001.0948.

一种公共巨细胞病毒特异性T细胞受体与其同源抗原复合物的结晶及初步X射线晶体学表征

Crystallization and preliminary X-ray crystallographic characterization of a public CMV-specific TCR in complex with its cognate antigen.

作者信息

Reiser Jean Baptiste, Legoux François, Machillot Paul, Debeaupuis Emilie, Le Moullac-Vaydie Béatrice, Chouquet Anne, Saulquin Xavier, Bonneville Marc, Housset Dominique

机构信息

Institut de Biologie Structurale Jean-Pierre Ebel, UMR, Grenoble, France.

出版信息

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2009 Nov 1;65(Pt 11):1157-61. doi: 10.1107/S1744309109037890. Epub 2009 Oct 30.

DOI:10.1107/S1744309109037890
PMID:19923740
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC2777048/
Abstract

The T-cell response to human cytomegalovirus is characterized by a dramatic reduction of clonal diversity in patients undergoing chronic inflammation or immunodepression. In order to check whether all the selected high-avidity T-cell clones recognize the immunodominant pp65 peptide antigen pp65(495-503) (NLVPMVATV) presented by the major histocompatibility complex (MHC) molecule HLA-A2 in a similar manner, several public high-affinity T-cell receptors (TCRs) specific for the pp65(495-503)-HLA-A2 complex have been investigated. Expression, purification and crystallization were performed and preliminary crystallographic data were collected to 4.7 angstrom resolution for the RA15 TCR in complex with the pp65(495-503)-HLA-A2 complex. Comparison of the RA15-pp65(495-503)-HLA-A2 complex molecular-replacement solution with the structure of another high-affinity pp65(495-503)-HLA-A2-specific TCR, RA14, shows a shared docking mode, indicating that the clonal focusing could be accompanied by the selection of a most favoured peptide-readout mode. However, the position of the RA15 V beta domain is significantly shifted, suggesting a different interatomic interaction network.

摘要

在经历慢性炎症或免疫抑制的患者中，T细胞对人巨细胞病毒的反应特征是克隆多样性显著降低。为了检查所有选定的高亲和力T细胞克隆是否以相似方式识别由主要组织相容性复合体（MHC）分子HLA - A2呈递的免疫显性pp65肽抗原pp65(495 - 503)（NLVPMVATV），已对几种针对pp65(495 - 503)-HLA - A2复合体的公共高亲和力T细胞受体（TCR）进行了研究。进行了表达、纯化和结晶，并收集了与pp65(495 - 503)-HLA - A2复合体结合的RA15 TCR的初步晶体学数据，分辨率达到4.7埃。将RA15-pp65(495 - 503)-HLA - A2复合体的分子置换溶液与另一种高亲和力的pp65(495 - 503)-HLA - A2特异性TCR即RA14的结构进行比较，结果显示存在共享的对接模式，这表明克隆聚焦可能伴随着最有利的肽读出模式的选择。然而，RA15 Vβ结构域的位置发生了显著偏移，这表明存在不同的原子间相互作用网络。