寡聚化噬菌体蛋白激活一种成孔型抗噬菌体防御，这一成果由多伦多大学Karen L. Maxwell研究组经过不懈努力而取得。这一研究成果发表在2026年2月4日出版的国际学术期刊《自然》上。

在这里，该课题组描述了一个164个残基的噬菌体编码蛋白，通过感知噬菌体组装的保守寡聚组分来保护细菌。这种蛋白被称为环相互作用孔1 (Rip1)，被感染噬菌体的入口蛋白或小端酶蛋白激活-寡聚环状复合物是病毒粒子成熟所必需的。Rip1将这些噬菌体蛋白环复合物作为模板组装成破坏膜的孔，从而抑制噬菌体病毒粒子组装和宿主细胞的过早死亡。Rip1同源物广泛分布在细菌中，并提供对各种噬菌体的有效防御。这项研究揭示了一种策略，通过利用病毒组装的保守特征，一个小的防御蛋白整合了传感和效应活性。该机制反映了真核生物的孔隙形成免疫，但由单一蛋白质执行，为病毒检测和防御提供了一种进化上简化的解决方案。

据介绍，细菌已经进化出一系列广泛的防御系统来对抗噬菌体感染，其中许多系统依赖于复杂的信号系统和大的蛋白质复合物来发挥作用。

附：英文原文

Title: A pore-forming antiphage defence is activated by oligomeric phage proteins

Author: Patel, Pramalkumar H., McCarthy, Matthew R., Taylor, Vronique L., Cole, Gregory B., Zhang, Chi, Edghill, Matthew M., Getz, Landon J., Fung, Beatrice C. M., Moraes, Trevor F., Davidson, Alan R., Norris, Michael J., Maxwell, Karen L.

Issue&Volume: 2026-02-04

Abstract: Bacteria have evolved a wide array of defence systems to combat phage infection, many of which rely on complex signalling systems and large protein complexes to function1. Here we describe a 164-residue prophage-encoded protein that defends bacteria by sensing conserved oligomeric components of phage assembly. This protein, called ring interacting pore 1 (Rip1), is activated by the portal or small terminase proteins of infecting phages—oligomeric ring-shaped complexes that are essential for virion maturation. Rip1 uses these phage protein ring complexes as a template to assemble into membrane-disrupting pores that inhibit phage virion assembly and cause premature death of the host cell. Rip1 homologues are widely distributed across bacteria and provide robust defence against diverse phages. This study reveals a strategy by which a small defence protein integrates both sensing and effector activity by exploiting a conserved feature of viral assembly. The mechanism mirrors eukaryotic pore-forming immunity but is executed by a single protein, offering an evolutionarily streamlined solution to viral detection and defence.

DOI: 10.1038/s41586-025-10075-1

Source: https://www.nature.com/articles/s41586-025-10075-1