Peptide presentation on MHC class I molecules (MHC-I) is central to mounting effective antiviral and antitumoral immune responses. The tapasin-related protein TAPBPR is an MHC-I peptide editor which shapes the final peptide repertoire displayed on the cell surface. Here, we review recent findings which further elucidate the mechanisms by which TAPBPR performs peptide editing on a molecular level, and how glycosylation on MHC-I influences the interaction with TAPBPR and the peptide loading complex. We also explore how the function of TAPBPR can be utilized to promote exogenous peptide loading directly onto plasma-membrane expressed MHC-I. This has led to the development of new assays to investigate TAPBPR-mediated peptide editing and uncovered translational opportunities of utilizing TAPBPR to treat human disease.

中文翻译：

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TAPBPR 的来龙去脉。

MHC I 类分子 (MHC-I) 上的肽呈递对于产生有效的抗病毒和抗肿瘤免疫反应至关重要。Tapasin 相关蛋白 TAPBPR 是一种 MHC-I 肽编辑器，可塑造在细胞表面展示的最终肽库。在这里，我们回顾了最近的发现，这些发现进一步阐明了 TAPBPR 在分子水平上进行肽编辑的机制，以及 MHC-I 上的糖基化如何影响与 TAPBPR 和肽加载复合物的相互作用。我们还探讨了如何利用 TAPBPR 的功能来促进外源肽直接加载到质膜表达的 MHC-I 上。这导致开发了新的检测方法来研究 TAPBPR 介导的肽编辑，并发现了利用 TAPBPR 治疗人类疾病的转化机会。