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Updated: Jun 26, 2025

Following Cell-fate in E. coli After Infection by Phage Lambda
Published on: October 14, 2011
Structural mechanism of bacteriophage lambda tail's interaction with the bacterial receptor
1State Key Laboratory of Membrane Biology, Beijing Frontier Research Center for Biological Structure, School of Life Sciences, Tsinghua University, 100084, Beijing, PR China.
Bacteriophage lambda uses its tail to bind the Shigella sonnei LamB receptor, triggering DNA injection. High-resolution cryo-EM structures reveal conformational changes in the phage tail upon binding, clarifying infection initiation.
Area of Science:
- Microbiology
- Structural Biology
- Virology
Background:
- Bacteriophage lambda infection begins with tail-mediated binding to bacterial receptors.
- The interaction between bacteriophage lambda and its receptor LamB is crucial but not fully understood at a molecular level.
Purpose of the Study:
- To elucidate the molecular mechanism of bacteriophage lambda infection initiation.
- To determine the high-resolution structures of bacteriophage lambda tail complexed with the LamB receptor.
Main Methods:
- High-resolution cryo-electron microscopy (cryo-EM).
- Structural analysis of bacteriophage lambda tail complexed with Shigella sonnei LamB receptor.
Main Results:
- Determined cryo-EM structures of bacteriophage lambda tail complexed with LamB receptor and central tail fiber.
- Revealed substantial conformational changes in the phage lambda tail tip upon LamB binding.
- Detailed the complex processes triggering phage infection.
Conclusions:
- The study provides detailed structural insights into bacteriophage lambda infection initiation.
- Understanding lambda-bacterial interactions is significant for microbiology and therapeutic development.
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