Cryo-EM structures of a Xanthomonas phage: Insights into viral architecture and implications for the model phage HK97

IF 4.4 2区生物学 Q2 BIOCHEMISTRY & MOLECULAR BIOLOGY

Structure Pub Date : 2025-04-23 DOI:10.1016/j.str.2025.03.013

Mingcheng Guo, Aohan Wang, Yaqi Zheng, Chaoying Liu, Qianqian Shao, Yunfei Deng, Lin Li, Yueting Wang, Xiaofang Wang, Yue Shen, Jun Qian, Xiaofeng Zhou, Qianglin Fang

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引用次数: 0

Abstract

Xanthomonas bacteria are responsible for disease outbreaks in several hundred plant species, causing significant economic losses. Xanthomonas phages have emerged as a promising biocontrol strategy in managing various important plant diseases caused by Xanthomonas bacteria. However, structural information for Xanthomonas phages has remained limited so far. Here, we present high-resolution cryo-electron microscopy (cryo-EM) structures of the Xanthomonas citri phage ΦXacJX1 from siphoviruses. These structures include atomic models for the head, head-to-tail connector and head-proximal portion of the tail. ΦXacJX1’s head and head-to-tail connector components show significant protein sequence and structural homology with those of the model siphophage HK97. However, the in-situ structures of head-to-tail connector of phage HK97 remain unavailable. The presented structures of phage ΦXacJX1 enhance our understanding of Xanthomonas phages and the mature virion of phage HK97. They provide a valuable framework for future structural and functional studies on both Xanthomonas phages and phage HK97.

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黄单胞菌噬菌体的低温电镜结构：对病毒结构的见解和对模型噬菌体HK97的影响

黄单胞菌是几百种植物爆发病害的罪魁祸首，造成重大经济损失。黄单胞菌噬菌体已成为管理黄单胞菌引起的各种重要植物病害的一种有前途的生物控制策略。然而，迄今为止，黄单胞菌噬菌体的结构信息仍然有限。在这里，我们展示了来自虹吸病毒的柠檬黄单胞菌噬菌体ΦXacJX1的高分辨率冷冻电镜（cryo-EM）结构。这些结构包括头部、头尾连接体和尾部头部近端部分的原子模型。ΦXacJX1的头部和头尾连接部分与虹彩病毒模型HK97的蛋白质序列和结构有显著的同源性。然而，HK97噬菌体头尾连接体的原位结构仍未获得。所展示的ΦXacJX1噬菌体结构增强了我们对黄单胞菌噬菌体和HK97噬菌体成熟病毒的了解。它们为今后对黄单胞菌噬菌体和HK97噬菌体进行结构和功能研究提供了一个宝贵的框架。

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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.