van Endert P M
INSERM U25, Hôpital Necker, Paris, France.
Immunol Res. 1996;15(4):265-79. doi: 10.1007/BF02935312.
Peptide epitopes presented by HLA class I are supplied by an elaborate system of antigen processing which subjects candidate epitopes to a process of selection according to little-understood rules. Transport of peptides from the cytosol into the endoplasmic reticulum by the TAP (transporter associated with antigen processing) complex is likely to play an important role in peptide selection for presentation. The recent development of an assay measuring substrate binding to the TAP complex has led to the identification of the major structural properties of peptides selected by the human transporter. Human TAP favors transport of peptides with structural features common to HLA class I ligands. However, TAP dislikes peptide ligands preferred by some HLA class I alleles, which may therefore frequently rely on alternative sources of peptide ligands.
HLA I类分子呈递的肽表位由一个精细的抗原加工系统提供,该系统会根据鲜为人知的规则,对候选表位进行筛选。通过TAP(抗原加工相关转运体)复合体将肽从胞质溶胶转运至内质网,这一过程可能在用于呈递的肽的选择中发挥重要作用。一种用于测量底物与TAP复合体结合的检测方法的最新进展,已使得人们能够鉴定出人类转运体所选择的肽的主要结构特性。人类TAP倾向于转运具有HLA I类配体共有的结构特征的肽。然而,TAP不喜欢某些HLA I类等位基因所偏好的肽配体,因此这些等位基因可能经常依赖肽配体的替代来源。