During phage infection, both virus and bacteria attempt to gain and/or maintain control over critical bacterial functions, through a plethora of strategies. These strategies include posttranslational modifications (PTMs, including phosphorylation, ribosylation, and acetylation), as rapid and dynamic regulators of protein behavior. However, to date, knowledge on the topic remains scarce and fragmented, while a more systematic investigation lies within reach. The release of AlphaFold, which advances PTM enzyme discovery and functional elucidation, and the increasing inclusivity and scale of mass spectrometry applications to new PTM types, could significantly accelerate research in the field. In this review, we highlight the current knowledge on PTMs during phage infection, and conceive a possible pipeline for future research, following an enzyme–target–function scheme.

在噬菌体感染期间，病毒和细菌都试图通过多种策略来获得和/或维持对关键细菌功能的控制。这些策略包括翻译后修饰（PTM，包括磷酸化、核糖基化和乙酰化），作为蛋白质行为的快速和动态调节剂。然而，迄今为止，有关该主题的知识仍然稀缺且支离破碎，而更系统的调查却触手可及。AlphaFold 的发布推动了 PTM 酶的发现和功能阐明，以及质谱应用对新 PTM 类型的包容性和规模的不断增加，可以显着加速该领域的研究。在这篇综述中，我们重点介绍了噬菌体感染过程中 PTM 的当前知识，并按照酶-靶标-功能方案设想了未来研究的可能途径。