霍乱弧菌分型荚膜 VP1 在两种状态下的三维结构

IF 4.4 2区生物学 Q2 BIOCHEMISTRY & MOLECULAR BIOLOGY

Structure Pub Date : 2024-10-28 DOI:10.1016/j.str.2024.10.005

Hao Pang, Fenxia Fan, Jing Zheng, Hao Xiao, Zhixue Tan, Jingdong Song, Biao Kan, Hongrong Liu

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引用次数: 0

摘要

溶解性荚膜噬菌体（VP1-VP5）在霍乱弧菌 O1 生物型 El Tor 的亚型鉴定中起着至关重要的作用。然而，到目前为止，这些噬菌体还没有任何结构，这阻碍了我们对感染和 DNA 释放的分子机制的了解。在这里，我们用冷冻电子显微镜（cryo-EM）测定了成熟的 VP1 结构和 DNA 释放的 VP1 结构，其分辨率分别接近原子和亚纳米。VP1 头部由 415 个拷贝的主要帽状蛋白 gp7 和 11 个塔形尖峰组成。VP1 尾部由一个适配器、一个喷嘴、一个细长的环和一个尾针组成，两侧是三个延伸纤维 I 和六个三聚体纤维 II。在 DNA 射出的 VP1 中，纤维 II 的构象变化可能会导致尾针和核心蛋白的释放，从而形成一个拉长的尾部通道。我们的结构让我们了解了带有尾针的荚膜病毒感染和 DNA 释放的分子机制。

本文章由计算机程序翻译，如有差异，请以英文原文为准。

Three-dimensional structures of Vibrio cholerae typing podophage VP1 in two states

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Three-dimensional structures of Vibrio cholerae typing podophage VP1 in two states

Lytic podophages (VP1–VP5) play crucial roles in subtyping Vibrio cholerae O1 biotype El Tor. However, until now no structures of these phages have been available, which hindered our understanding of the molecular mechanisms of infection and DNA release. Here, we determined the cryoelectron microscopy (cryo-EM) structures of mature and DNA-ejected VP1 structures at near-atomic and subnanometer resolutions, respectively. The VP1 head is composed of 415 copies of the major capsid protein gp7 and 11 turret-shaped spikes. The VP1 tail consists of an adapter, a nozzle, a slender ring, and a tail needle, and is flanked by three extended fibers I and six trimeric fibers II. Conformational changes of fiber II in DNA-ejected VP1 may cause the release of the tail needle and core proteins, forming an elongated tail channel. Our structures provide insights into the molecular mechanisms of infection and DNA release for podophages with a tail needle.

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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.