Emory Vaccine Center, Emory University School of Medicine, Atlanta, Georgia.
Yerkes National Primate Research Center, Atlanta, Georgia.
Curr Protoc. 2021 Feb;1(2):e36. doi: 10.1002/cpz1.36.
Class II major histocompatibility complex peptide (MHC-IIp) multimers are precisely engineered reagents used to detect T cells specific for antigens from pathogens, tumors, and self-proteins. While the related Class I MHC/peptide (MHC-Ip) multimers are usually produced from subunits expressed in E. coli, most Class II MHC alleles cannot be produced in bacteria, and this has contributed to the perception that MHC-IIp reagents are harder to produce. Herein, we present a robust constitutive expression system for soluble biotinylated MHC-IIp proteins that uses stable lentiviral vector-transduced derivatives of HEK-293T cells. The expression design includes allele-specific peptide ligands tethered to the amino-terminus of the MHC-II β chain via a protease-cleavable linker. Following cleavage of the linker, HLA-DM is used to catalyze efficient peptide exchange, enabling high-throughput production of many distinct MHC-IIp complexes from a single production cell line. Peptide exchange is monitored using either of two label-free methods, native isoelectric focusing gel electrophoresis or matrix-assisted laser desorption/ionization time-of-flight (MALDI-TOF) mass spectrometry of eluted peptides. Together, these methods produce MHC-IIp complexes that are highly homogeneous and that form the basis for excellent MHC-IIp multimer reagents. © 2021 Wiley Periodicals LLC. Basic Protocol 1: Lentivirus production and expression line creation Support Protocol 1: Six-well assay for estimation of production cell line yield Support Protocol 2: Universal ELISA for quantifying proteins with fused leucine zippers and His-tags Basic Protocol 2: Cultures for production of Class II MHC proteins Basic Protocol 3: Purification of Class II MHC proteins by anti-leucine zipper affinity chromatography Alternate Protocol 1: IMAC purification of His-tagged Class II MHC Support Protocol 3: Protein concentration measurements and adjustments Support Protocol 4: Polishing purification by anion-exchange chromatography Support Protocol 5: Estimating biotinylation percentage by streptavidin precipitation Basic Protocol 4: Peptide exchange Basic Protocol 5: Analysis of peptide exchange by matrix-assisted laser desorption/ionization (MALDI) mass spectrometry Alternate Protocol 2: Native isoelectric focusing to validate MHC-II peptide loading Basic Protocol 6: Multimerization Basic Protocol 7: Staining cells with Class II MHC tetramers.
II 类主要组织相容性复合物肽 (MHC-IIp) 多聚体是经过精确设计的试剂,用于检测针对病原体、肿瘤和自身蛋白的抗原的 T 细胞。虽然相关的 I 类 MHC/肽 (MHC-Ip) 多聚体通常由大肠埃希菌中表达的亚基产生,但大多数 II 类 MHC 等位基因不能在细菌中产生,这导致人们认为 MHC-IIp 试剂更难生产。在此,我们提出了一种稳健的可溶性生物素化 MHC-IIp 蛋白组成型表达系统,该系统使用稳定的慢病毒载体转导的 HEK-293T 细胞衍生物。该表达设计包括通过蛋白酶可切割接头连接到 MHC-IIβ 链氨基末端的等位基因特异性肽配体。接头切割后,使用 HLA-DM 催化有效的肽交换,从而能够从单个生产细胞系中高通量生产许多不同的 MHC-IIp 复合物。使用两种无标记方法之一监测肽交换,即天然等电聚焦凝胶电泳或洗脱肽的基质辅助激光解吸/电离飞行时间 (MALDI-TOF) 质谱法。这两种方法一起产生高度均一的 MHC-IIp 复合物,为出色的 MHC-IIp 多聚体试剂奠定了基础。© 2021 年 Wiley 期刊 LLC。基本方案 1:慢病毒生产和表达系创建支持方案 1:六孔板测定法估计生产细胞系产量支持方案 2:通用 ELISA 用于定量融合亮氨酸拉链和 His 标签的蛋白质基本方案 2:II 类 MHC 蛋白的培养基本方案 3:通过抗亮氨酸拉链亲和层析纯化 II 类 MHC 蛋白替代方案 1:His 标记的 II 类 MHC 的 IMAC 纯化支持方案 3:蛋白质浓度测量和调整支持方案 4:阴离子交换层析的抛光纯化支持方案 5:通过链霉亲和素沉淀估计生物素化百分比基本方案 4:肽交换基本方案 5:基质辅助激光解吸/电离 (MALDI) 质谱法分析肽交换替代方案 2:验证 MHC-II 肽加载的原生等电聚焦基本方案 6:多聚化基本方案 7:用 II 类 MHC 四聚体染色细胞。