Academic Journal
A receptor-centered approach identifies Lom as a LamB-bound superinfection exclusion factor in bacteriophage λ.
| Τίτλος: | A receptor-centered approach identifies Lom as a LamB-bound superinfection exclusion factor in bacteriophage λ. |
|---|---|
| Συγγραφείς: | Ge X; State Key Laboratory of Membrane Biology, Beijing Frontier Research Center for Biological Structure, School of Life Sciences, Tsinghua University, Beijing 100084, P.R. China; Health and Wellness, City University of Macau, Macau 999078, P.R. China. Electronic address: gxf16@tsinghua.org.cn., Gu Z; State Key Laboratory of Membrane Biology, Beijing Frontier Research Center for Biological Structure, School of Life Sciences, Tsinghua University, Beijing 100084, P.R. China., 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: | Cell reports [Cell Rep] 2026 Jul 28; Vol. 45 (7), pp. 117691. Date of Electronic Publication: 2026 Jul 17. |
| Τύπος έκδοσης: | Journal Article |
| Γλώσσα: | English |
| Στοιχεία περιοδικού: | Publisher: Cell Press Country of Publication: United States NLM ID: 101573691 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 2211-1247 (Electronic) NLM ISO Abbreviation: Cell Rep Subsets: MEDLINE |
| Imprint Name(s): | Original Publication: [Cambridge, MA] : Cell Press, c 2012- |
| Ιατρικοί όροι (MeSH): | Bacteriophage lambda*/metabolism , Bacteriophage lambda*/physiology , Bacterial Outer Membrane Proteins*/metabolism , Bacterial Outer Membrane Proteins*/chemistry , Porins*/metabolism , Porins*/chemistry , Superinfection*, Viral Proteins/metabolism ; Escherichia coli/virology ; Escherichia coli/metabolism ; Protein Binding ; Receptors, Virus |
| Περίληψη: | Bacteriophages face intense competition within bacterial populations. Although bacteria encode diverse anti-phage mechanisms, strategies protecting virions at the host surface remain poorly understood. Here, we develop a receptor-centered discovery approach that captures phage proteins bound to host receptors during infection. Applying this strategy to bacteriophage λ and its outer-membrane receptor LamB, we identify Lom as a phage-encoded outer membrane protein that binds LamB. Structural, biochemical, and functional analyses show that Lom occupies the same LamB surface recognized by the receptor-binding protein gpJ, thereby reducing phage adsorption through receptor occlusion. Ribosome profiling indicates that lom is strongly expressed during late lytic growth and is also expressed during lysogeny, consistent with a role in receptor-level superinfection exclusion. Foldseek analyses identify structurally related Lom-like proteins in diverse temperate phages, raising the possibility that receptor occlusion is a more widespread strategy. These findings establish a framework for discovering receptor-level phage competition mechanisms. (Copyright © 2026 The Authors. Published by Elsevier Inc. All rights reserved.) |
| Competing Interests: | Declaration of interests The authors declare no competing interests. |
| Contributed Indexing: | Keywords: CP: microbiology; LamB; Lom; anti-phage; bacteriophage λ; cryo-EM; membrane protein; superinfection exclusion |
| Substance Nomenclature: | 0 (maltoporins) 0 (Bacterial Outer Membrane Proteins) 0 (Porins) 0 (Viral Proteins) 0 (Receptors, Virus) |
| Entry Date(s): | Date Created: 20260717 Date Completed: 20260730 Latest Revision: 20260730 |
| Update Code: | 20260730 |
| DOI: | 10.1016/j.celrep.2026.117691 |
| PMID: | 42467530 |
| Βάση Δεδομένων: | MEDLINE |
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