The identification of peptides bound to human leukocyte antigen class I (HLA‐I) molecules—that is, the HLA‐I immunopeptidome—is a useful tool in the hunt for epitopes suitable for vaccinations and immunotherapies. These peptides are mainly generated by proteasomes through peptide hydrolysis and peptide splicing. In this issue, Nicastri and colleagues compared different methods for the elution of HLA class I‐associated peptides. It is demonstrated that the choice of HLA‐associated peptide enrichment and purification strategy affects peptide yields and creates a bias in detected sequence repertoire. The author carried out this technical brief through the analysis of canonical non‐spliced peptides. However, their study left out any analysis of post‐translationally spliced peptides, thereby missing an opportunity to shed light on the persistent debate of the frequency of these unconventional peptides.

中文翻译：

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我们在 HLA I 类免疫肽组中看到什么、看不到什么以及我们不想看到什么。


识别与人类白细胞抗原 I 类 (HLA-I) 分子结合的肽（即 HLA-I 免疫肽组）是寻找适合疫苗接种和免疫治疗的表位的有用工具。这些肽主要由蛋白酶体通过肽水解和肽剪接产生。在本期中，Nicatri 及其同事比较了 HLA I 类相关肽的不同洗脱方法。事实证明，HLA 相关肽富集和纯化策略的选择会影响肽产量，并在检测到的序列库中产生偏差。作者通过对典型非剪接肽的分析来完成本技术简介。然而，他们的研究遗漏了对翻译后剪接肽的任何分析，从而错过了阐明这些非常规肽频率的持续争论的机会。