Mesh : Bacteriophage lambda / genetics metabolism physiology Cryoelectron Microscopy Shigella sonnei / virology metabolism Viral Tail Proteins / metabolism chemistry genetics Porins / metabolism chemistry Bacterial Outer Membrane Proteins / metabolism chemistry ultrastructure Protein Binding Models, Molecular Protein Conformation Receptors, Virus

来  源:   DOI:10.1038/s41467-024-48686-3   PDF(Pubmed)

Abstract:
Bacteriophage infection, a pivotal process in microbiology, initiates with the phage\'s tail recognizing and binding to the bacterial cell surface, which then mediates the injection of viral DNA. Although comprehensive studies on the interaction between bacteriophage lambda and its outer membrane receptor, LamB, have provided rich information about the system\'s biochemical properties, the precise molecular mechanism remains undetermined. This study revealed the high-resolution cryo-electron microscopy (cryo-EM) structures of the bacteriophage lambda tail complexed with its irreversible Shigella sonnei 3070 LamB receptor and the closed central tail fiber. These structures reveal the complex processes that trigger infection and demonstrate a substantial conformational change in the phage lambda tail tip upon LamB binding. Providing detailed structures of bacteriophage lambda infection initiation, this study contributes to the expanding knowledge of lambda-bacterial interaction, which holds significance in the fields of microbiology and therapeutic development.
摘要:
噬菌体感染,微生物学中的一个关键过程,启动与噬菌体的尾巴识别和结合到细菌细胞表面,然后介导病毒DNA的注射。尽管对噬菌体λ与其外膜受体之间的相互作用进行了全面的研究,LamB,提供了有关系统生化特性的丰富信息,精确的分子机制仍未确定。这项研究揭示了噬菌体λ尾的高分辨率低温电子显微镜(cryo-EM)结构与其不可逆的志贺氏菌3070LamB受体和封闭的中央尾纤维复合。这些结构揭示了触发感染的复杂过程,并在LamB结合后证明了噬菌体λ尾尖的实质性构象变化。提供噬菌体λ感染起始的详细结构,这项研究有助于扩大λ-细菌相互作用的知识,这在微生物学和治疗发展领域具有重要意义。
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