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Abstract：
Cellular compartmentalization of proteins and protein complex formation allow cells to tightly control biological processes. Therefore, understanding the subcellular localization and interactions of a specific protein is crucial to uncover its biological function. The advent of proximity labeling (PL) has reshaped cellular proteomics in infection biology. PL utilizes a genetically modified enzyme that generates a \"labeling cloud\" by covalently labeling proteins in close proximity to the enzyme. Fusion of a PL enzyme to a specific antibody or a \"bait\" protein of interest in combination with affinity enrichment mass spectrometry (AE-MS) enables the isolation and identification of the cellular proximity proteome, or proxisome. This powerful methodology has been paramount for the mapping of membrane or membraneless organelles as well as for the understanding of hard-to-purify protein complexes, such as those of transmembrane proteins. Unsurprisingly, more and more infection biology research groups have recognized the potential of PL for the identification of host-pathogen interactions. In this chapter, we introduce the enzymes commonly used for PL labeling as well as recent promising advancements and summarize the major achievements in organelle mapping and nucleic acid PL. Moreover, we comprehensively describe the research on host-pathogen interactions using PL, giving special attention to studies in the field of virology.
摘要：
蛋白质的细胞区室化和蛋白质复合物的形成允许细胞严格控制生物过程。因此,了解特定蛋白质的亚细胞定位和相互作用对于揭示其生物学功能至关重要。邻近标记（PL）的出现重塑了感染生物学中的细胞蛋白质组学。PL利用一种基因修饰的酶，通过共价标记靠近酶的蛋白质来产生“标记云”。PL酶与特定抗体或“诱饵”蛋白的融合结合亲和富集质谱（AE-MS）可以分离和鉴定细胞邻近蛋白质组，或者proxisome.这种强大的方法对于膜或无膜细胞器的定位以及对难以纯化的蛋白质复合物的理解至关重要。例如跨膜蛋白。毫不奇怪,越来越多的感染生物学研究小组已经认识到PL在鉴定宿主-病原体相互作用方面的潜力。在这一章中,我们介绍了常用于PL标记的酶以及最近有希望的进展，并总结了细胞器作图和核酸PL的主要成就。此外，我们全面描述了使用PL对宿主-病原体相互作用的研究，特别关注病毒学领域的研究。
