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Structural mechanism of bacteriophage lambda tail’s interaction with the bacterial receptor
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Journal Article
Structural mechanism of bacteriophage lambda tail’s interaction with the bacterial receptor
2024
Overview
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.
Publisher
Nature Publishing Group UK,Nature Publishing Group,Nature Portfolio
Subject
/ 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
/ Humanities and Social Sciences
/ Phages
/ Science
/ Shigella sonnei - metabolism
/ Transmission electron microscopy
/ Viral Tail Proteins - chemistry
