Structures of a T1-like siphophage reveal capsid stabilization mechanisms and high structural similarities with a myophage

IF 4.3 2区生物学 Q2 BIOCHEMISTRY & MOLECULAR BIOLOGY Structure Pub Date : 2025-02-05 DOI:10.1016/j.str.2025.01.012

Can Cai, Yueting Wang, Yunshu Liu, Qianqian Shao, Aohan Wang, Lin Li, Yaqi Zheng, Tianyi Zhang, Ziwen Luo, Chongguang Yang, Qianglin Fang

引用次数: 0

Abstract

Bacteriophage T1, a member of Siphoviruses, infects Escherichia coli with high efficiency, making it a promising candidate for phage therapy. Here, we report the near-atomic structures of FCWL1, a T1-like phage that belongs to the T1 phage family. We focus on the head, the head-to-tail interface, and its surrounding components. The hexameric capsomer displays unique gaps between neighboring A domains of the major capsid proteins. These gaps are partially filled by the N-loop of the decoration protein, which adopts a unique conformation. These structural features suggest that the phage might employ a novel strategy for stabilizing its head. Furthermore, despite being a siphophage, the head and head-to-tail connector of the phage show high structural similarity to those of a myophage. These findings enhance our understanding of the structure, capsid stabilization mechanism, and evolution of phages in the T1 family.

Abstract Image

查看原文

微信好友朋友圈 QQ好友复制链接

本刊更多论文

t1样噬菌体的结构揭示了衣壳稳定机制和与肌噬体的高度结构相似性

噬菌体T1是虹膜病毒的一员，它能高效感染大肠杆菌，是噬菌体治疗的一个很有前途的候选噬菌体。在这里，我们报道了FCWL1的近原子结构，这是一种属于T1噬菌体家族的T1样噬菌体。我们关注的是头部，头部到尾部的接口，以及它周围的组件。六聚体衣壳体在主要衣壳蛋白的相邻A结构域之间显示出独特的间隙。这些间隙部分由装饰蛋白的n环填充，它采用独特的构象。这些结构特征表明，噬菌体可能采用了一种新的策略来稳定其头部。此外，尽管是一个噬菌体，噬菌体的头部和从头到尾的连接器显示出与myophage高度相似的结构。这些发现增强了我们对T1家族噬菌体的结构、衣壳稳定机制和进化的理解。

本文章由计算机程序翻译，如有差异，请以英文原文为准。

求助全文

约1分钟内获得全文去求助

来源期刊

Structure 生物-生化与分子生物学

CiteScore

8.90

自引率

1.80%

发文量

155

审稿时长

3-8 weeks

期刊介绍： Structure aims to publish papers of exceptional interest in the field of structural biology. The journal strives to be essential reading for structural biologists, as well as biologists and biochemists that are interested in macromolecular structure and function. Structure strongly encourages the submission of manuscripts that present structural and molecular insights into biological function and mechanism. Other reports that address fundamental questions in structural biology, such as structure-based examinations of protein evolution, folding, and/or design, will also be considered. We will consider the application of any method, experimental or computational, at high or low resolution, to conduct structural investigations, as long as the method is appropriate for the biological, functional, and mechanistic question(s) being addressed. Likewise, reports describing single-molecule analysis of biological mechanisms are welcome. In general, the editors encourage submission of experimental structural studies that are enriched by an analysis of structure-activity relationships and will not consider studies that solely report structural information unless the structure or analysis is of exceptional and broad interest. Studies reporting only homology models, de novo models, or molecular dynamics simulations are also discouraged unless the models are informed by or validated by novel experimental data; rationalization of a large body of existing experimental evidence and making testable predictions based on a model or simulation is often not considered sufficient.