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-Structure paper
| タイトル | Structures of λ-like phage A8 tail tip bound to OmpC provide insight into receptor recognition. |
|---|---|
| ジャーナル・号・ページ | Structure, Year 2026 |
| 掲載日 | 2026年2月27日 |
著者 | Tingyue Deng / Xiaofei Ge / Jiawei Wang / ![]() |
| PubMed 要旨 | 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. |
リンク | Structure / PubMed:41763202 |
| 手法 | EM (単粒子) |
| 解像度 | 3.49 - 3.89 Å |
| 構造データ | EMDB-65858, PDB-9wca: EMDB-65859, PDB-9wcb: |
| 由来 |
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キーワード | VIRAL PROTEIN / Phage Tail |
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Lambdavirus (ウイルス)
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