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| Title | Structures of λ-like phage A8 tail tip bound to OmpC provide insight into receptor recognition. |
|---|---|
| Journal, issue, pages | Structure, Year 2026 |
| Publish date | Feb 27, 2026 |
 Authors | Tingyue Deng / Xiaofei Ge / Jiawei Wang /  |
| PubMed Abstract | Bacteriophage infection begins with the specific recognition of bacterial surface receptors by tail tip proteins, a decisive event that determines host specificity and triggers genome delivery. ...Bacteriophage infection begins with the specific recognition of bacterial surface receptors by tail tip proteins, a decisive event that determines host specificity and triggers genome delivery. However, the structural principles underlying this process remain poorly understood. Here, we determined high-resolution cryo-electron microscopy (cryo-EM) structures of the engineered λ-like bacteriophage A8 gpJ713 in the unbound form and bound to the outer membrane porin OmpC. Comparisons with our previously determined structures of wild-type λ gpJ alone and bound to LamB reveal conserved receptor binding-induced conformational transitions across λ-like siphoviruses, defining a general mechanistic framework for tail-tip recognition. Guided by this framework, we restored stable binding to the previously incompatible OmpC G40 variant and converted OmpF into a functional receptor through a minimal loop deletion. These proof-of-concept receptor reprogramming experiments demonstrate the predictive power of our structural model and illustrate how targeted receptor engineering can complement directed evolution in developing therapeutic phages. |
 External links | Structure / PubMed:41763202 |
| Methods | EM (single particle) |
| Resolution | 3.49 - 3.89 Å |
| Structure data | EMDB-65858, PDB-9wca: EMDB-65859, PDB-9wcb: |
| Source |
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 Keywords | VIRAL PROTEIN / Phage Tail |
Lambdavirus
escherichia coli o157:h7 str. edl933 (bacteria)