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伴侣分子和催化剂：抗原呈递途径如何应对生物学需求。

Chaperones and Catalysts: How Antigen Presentation Pathways Cope With Biological Necessity.

机构信息

Laboratory of Immune System Biology, National Institute of Allergy and Infectious Diseases, Molecular Biology Section, National Institutes of Health, Bethesda, MD, United States.

出版信息

Front Immunol. 2022 Apr 7;13:859782. doi: 10.3389/fimmu.2022.859782. eCollection 2022.

DOI:10.3389/fimmu.2022.859782
PMID:35464465
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC9022212/
Abstract

Immune recognition by T lymphocytes and natural killer (NK) cells is in large part dependent on the identification of cell surface MHC molecules bearing peptides generated from either endogenous (MHC I) or exogenous (MHC II) dependent pathways. This review focuses on MHC I molecules that coordinately fold to bind self or foreign peptides for such surface display. Peptide loading occurs in an antigen presentation pathway that includes either the multimolecular peptide loading complex (PLC) or a single chain chaperone/catalyst, TAP binding protein, related, TAPBPR, that mimics a key component of the PLC, tapasin. Recent structural and dynamic studies of TAPBPR reveal details of its function and reflect on mechanisms common to tapasin. Regions of structural conservation among species suggest that TAPBPR and tapasin have evolved to satisfy functional complexities demanded by the enormous polymorphism of MHC I molecules. Recent studies suggest that these two chaperone/catalysts exploit structural flexibility and dynamics to stabilize MHC molecules and facilitate peptide loading.

摘要

T 淋巴细胞和自然杀伤 (NK) 细胞的免疫识别在很大程度上依赖于对细胞表面 MHC 分子的识别，这些分子携带有源自内源性 (MHC I) 或外源性 (MHC II) 途径的肽。本文重点介绍 MHC I 分子，这些分子协调折叠以结合自身或外来肽进行表面展示。肽加载发生在抗原呈递途径中，该途径包括多分子肽加载复合物 (PLC) 或单链伴侣/催化剂 TAP 结合蛋白 (TAPBP) 相关蛋白，TAPBPR，它模拟 PLC 的关键成分 tapasin。最近对 TAPBPR 的结构和动态研究揭示了其功能的细节，并反映了 tapasin 的共同机制。物种间结构保守区域表明，TAPBPR 和 tapasin 已经进化以满足 MHC I 分子巨大多态性所要求的功能复杂性。最近的研究表明，这两种伴侣/催化剂利用结构灵活性和动力学来稳定 MHC 分子并促进肽加载。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/4a4b/9022212/8b645dfdee7e/fimmu-13-859782-g006.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/4a4b/9022212/64d3ba9970b9/fimmu-13-859782-g001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/4a4b/9022212/57e785ed2e15/fimmu-13-859782-g002.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/4a4b/9022212/08a69d04c422/fimmu-13-859782-g003.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/4a4b/9022212/aa9e0d2ee4c8/fimmu-13-859782-g004.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/4a4b/9022212/6e14ea5b2919/fimmu-13-859782-g005.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/4a4b/9022212/8b645dfdee7e/fimmu-13-859782-g006.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/4a4b/9022212/64d3ba9970b9/fimmu-13-859782-g001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/4a4b/9022212/57e785ed2e15/fimmu-13-859782-g002.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/4a4b/9022212/08a69d04c422/fimmu-13-859782-g003.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/4a4b/9022212/aa9e0d2ee4c8/fimmu-13-859782-g004.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/4a4b/9022212/6e14ea5b2919/fimmu-13-859782-g005.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/4a4b/9022212/8b645dfdee7e/fimmu-13-859782-g006.jpg

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