Structural mechanism of bacteriophage lambda tail’s interaction with the bacterial receptor

• Published in: Nature communications Vol. 15; no. 1; pp. 4185 - 11
• Main Authors: Ge, Xiaofei, Wang, Jiawei
• Format: Journal Article
• Language: English
• Published: London Nature Publishing Group UK 17.05.2024; Nature Publishing Group; Nature Portfolio
• Subjects: 101/28; 631/326/596/2557; 631/326/596/432; 631/535/1258/1259; Bacteria; Bacterial Outer Membrane Proteins - chemistry; Bacterial Outer Membrane Proteins - metabolism; Bacterial Outer Membrane Proteins - ultrastructure; Bacteriophage lambda - genetics; Bacteriophage lambda - metabolism; Bacteriophage lambda - physiology; Binding; Cell surface; Cell surface receptors; Cryoelectron Microscopy; Electron microscopy; Humanities and Social Sciences; Infections; Microbiology; Microscopy; Models, Molecular; Molecular modelling; multidisciplinary; Phages; Porins - chemistry; Porins - metabolism; Protein Binding; Protein Conformation; Receptors; Receptors, Virus; Science; Science (multidisciplinary); Shigella sonnei; Shigella sonnei - metabolism; Shigella sonnei - virology; Transmission electron microscopy; Viral Tail Proteins - chemistry; Viral Tail Proteins - genetics; Viral Tail Proteins - metabolism
• DOI: 10.1038/s41467-024-48686-3
• ISSN: 2041-1723

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. Here, Ge et al use cryo-electron microscopy to resolve the structure of the bacteriophage lambda tail in complex with its LamB receptor from Shigella sonnei and shed light on the conformational changes that the phage tail fiber undergoes in response to binding.