美国麻省理工学院Michael T. Laub团队的最新研究揭示了噬菌体触发超分子组装激活细菌免疫。相关论文于2026年2月4日发表于国际顶尖学术期刊《自然》杂志上。

在这里，该团队证明了细菌免疫蛋白环激活锌指RNase（RAZR）在两个不相关的噬菌体蛋白（假设的重组酶和门脉蛋白）形成的大环结构的圆周周围组装成一个活性的24 meric环。每一个多层、巨噬子规模的复合体使RAZR能够非特异性地切割RNA，以抑制翻译和限制噬菌体的繁殖。识别不相关的噬菌体蛋白，形成直径相似的环，表明这些蛋白质不仅与RAZR结合，而且还加强了对激活至关重要的几何形状。宿主体内缺乏大环结构可能会在感染前阻止自身免疫和RAZR激活。感染引发的RAZR寡聚化反映了真核天然免疫复合物中病原体诱导的寡聚化，强调了生物学中免疫的共同原则。

研究人员表示，细菌通过多种机制保护自己免受噬菌体的侵害。许多抗噬菌体系统形成大的寡聚复合物，但在噬菌体感染过程中寡聚是如何调节的仍然是未知的。

附：英文原文

Title: Bacterial immune activation via supramolecular assembly with phage triggers

Author: Zhang, Tong, Lyu, Yifei, Beck, Christina R., Iqbal, Naseer, Barbosa, Renee, Ghanbarpour, Alireza, Laub, Michael T.

Issue&Volume: 2026-02-04

Abstract: Bacteria use diverse mechanisms to protect themselves against phages1,2,3,4,5,6. Many antiphage systems form large oligomeric complexes, but how oligomerization is regulated during phage infection remains mostly unknown7,8,9,10,11,12. Here we demonstrate that the bacterial immunity protein ring-activated zinc-finger RNase (RAZR) assembles into an active, 24-meric ring around the circumference of large ring structures formed by two unrelated phage proteins: a putative recombinase and a portal protein. Each multi-layered, megadalton-scale complex enables RAZR to cleave RNA nonspecifically to inhibit translation and restrict phage propagation. The recognition of unrelated phage proteins that form rings with similar diameters indicates that these proteins not only bind to RAZR but also enforce a geometry crucial to activation. The lack of large ring structures in the host probably prevents auto-immunity and RAZR activation before infection. The infection-triggered oligomerization of RAZR mirrors pathogen-induced oligomerization in eukaryotic innate immune complexes13, underscoring a common principle of immunity across biology.

DOI: 10.1038/s41586-025-10060-8

Source: https://www.nature.com/articles/s41586-025-10060-8