Academic Journal
Structures of λ-like phage A8 tail tip bound to OmpC provide insight into receptor recognition.
| Τίτλος: | Structures of λ-like phage A8 tail tip bound to OmpC provide insight into receptor recognition. |
|---|---|
| Συγγραφείς: | Deng T; State Key Laboratory of Membrane Biology, Beijing Frontier Research Center for Biological Structure, School of Life Sciences, Tsinghua University, Beijing 100084, P.R. China., Ge X; Health and Wellness, City University of Macau, Macau 999078, P.R. China. Electronic address: gxf16@tsinghua.org.cn., Wang J; State Key Laboratory of Membrane Biology, Beijing Frontier Research Center for Biological Structure, School of Life Sciences, Tsinghua University, Beijing 100084, P.R. China. Electronic address: jwwang@tsinghua.edu.cn. |
| Πηγή: | Structure (London, England : 1993) [Structure] 2026 May 07; Vol. 34 (5), pp. 790-797.e3. Date of Electronic Publication: 2026 Feb 27. |
| Τύπος έκδοσης: | Journal Article |
| Γλώσσα: | English |
| Στοιχεία περιοδικού: | Publisher: Cell Press Country of Publication: United States NLM ID: 101087697 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1878-4186 (Electronic) Linking ISSN: 09692126 NLM ISO Abbreviation: Structure Subsets: MEDLINE |
| Imprint Name(s): | Publication: 2000- : Cambridge, Mass. : Cell Press Original Publication: London : Current Biology, c1993- |
| Ιατρικοί όροι (MeSH): | Porins*/metabolism , Porins*/chemistry , Porins*/genetics , Bacterial Outer Membrane Proteins*/metabolism , Bacterial Outer Membrane Proteins*/chemistry , Bacterial Outer Membrane Proteins*/genetics , Viral Tail Proteins*/metabolism , Viral Tail Proteins*/chemistry , Viral Tail Proteins*/genetics , Bacteriophage lambda*/metabolism , Bacteriophage lambda*/chemistry, Escherichia coli/metabolism ; Escherichia coli/virology ; Cryoelectron Microscopy ; Models, Molecular ; Protein Binding ; Binding Sites |
| Περίληψη: | 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. (Copyright © 2026 Elsevier Inc. All rights reserved.) |
| Competing Interests: | Declaration of interests The authors declare no competing interests. |
| Contributed Indexing: | Keywords: LamB; OmpC; OmpF; bacteriophage; cryo-EM; receptor recognition mechanisms; tail spike |
| Substance Nomenclature: | 0 (Porins) 0 (Bacterial Outer Membrane Proteins) 0 (OmpC protein) 0 (Viral Tail Proteins) 0 (OmpF protein) |
| Entry Date(s): | Date Created: 20260228 Date Completed: 20260710 Latest Revision: 20260710 |
| Update Code: | 20260711 |
| DOI: | 10.1016/j.str.2026.02.002 |
| PMID: | 41763202 |
| Βάση Δεδομένων: | MEDLINE |
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