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通过圆二色光谱法测定的异源三聚体pMHC蛋白的热稳定性

Thermal Stability of Heterotrimeric pMHC Proteins as Determined by Circular Dichroism Spectroscopy.

作者信息

Fuller Anna, Wall Aaron, Crowther Michael D, Lloyd Angharad, Zhurov Alexei, Sewell Andrew K, Cole David K, Beck Konrad

机构信息

Division of Infection and Immunity and Systems Immunity Research Institute, Cardiff University School of Medicine, Heath Park, Cardiff, UK.

Cardiff University School of Dentistry, Heath Park, Cardiff, UK.

出版信息

Bio Protoc. 2017 Jul 5;7(13). doi: 10.21769/BioProtoc.2366.

Abstract

T cell receptor (TCR) recognition of foreign peptide fragments, presented by peptide major histocompatibility complex (pMHC), governs T-cell mediated protection against pathogens and cancer. Many factors govern T-cell sensitivity, including the affinity of the TCR-pMHC interaction and the stability of pMHC on the surface of antigen presenting cells. These factors are particularly relevant for the peptide vaccination field, in which more stable pMHC interactions could enable more effective protection against disease. Here, we discuss a method for the determination of pMHC stability that we have used to investigate HIV immune escape, T-cell sensitivity to cancer antigens and mechanisms leading to autoimmunity.

摘要

T细胞受体(TCR)识别由肽主要组织相容性复合体(pMHC)呈递的外来肽片段,决定了T细胞介导的针对病原体和癌症的保护作用。许多因素决定了T细胞的敏感性,包括TCR-pMHC相互作用的亲和力以及pMHC在抗原呈递细胞表面的稳定性。这些因素对于肽疫苗接种领域尤为重要,在该领域中,更稳定的pMHC相互作用能够实现更有效的疾病预防。在此,我们讨论一种用于确定pMHC稳定性的方法,我们已使用该方法来研究HIV免疫逃逸、T细胞对癌症抗原的敏感性以及导致自身免疫的机制。

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