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TitleStructural basis of bacteriophage Ur-lambda infection initiation.
Journal, issue, pagesSci Adv, Vol. 11, Issue 46, Page eadw7914, Year 2025
Publish dateNov 14, 2025
AuthorsHuaxin Yu / Chunyan Wang / Jian Yue / Wangbiao Guo / Ian J Molineux / Jun Liu /
PubMed AbstractBacteriophages must recognize host receptors and penetrate the host cell envelope to initiate infection. How the classic phage λ initiates infection is not yet understood. Here, we combine cryo- ...Bacteriophages must recognize host receptors and penetrate the host cell envelope to initiate infection. How the classic phage λ initiates infection is not yet understood. Here, we combine cryo-electron microscopy and tomography to visualize infection initiation by Ur-λ, the original λ isolate that uses side fibers to adsorb rapidly to . We determine the structure of Ur-λ, resolving the full-length central and side fibers, thus providing a structural basis for host recognition. We show that Ur-λ contains six copies of its tape measure protein. We capture intermediates of the tail tip complex during infection initiation, revealing how extensive conformational changes enable adsorption, and visualize the trans-envelope channel required for genome ejection.
External linksSci Adv / PubMed:41237242 / PubMed Central
MethodsEM (single particle)
Resolution3.31 - 3.37 Å
Structure data

47685

9e7m

EMDB-47685, PDB-9e7m:
In situ cryoEM structure of bacteriophage Ur-lambda tail tip complex
Method: EM (single particle) / Resolution: 3.37 Å

48256

9mgh

EMDB-48256, PDB-9mgh:
In situ cryo-EM structure of bacteriophage Ur-lambda tail side fiber
Method: EM (single particle) / Resolution: 3.31 Å

Chemicals

ChemComp-SF4:
IRON/SULFUR CLUSTER

Source
  • escherichia phage lambda (virus)
KeywordsVIRAL PROTEIN / bacteriophage / tail tip complex

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