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| Title | A receptor-centered approach identifies Lom as a LamB-bound superinfection exclusion factor in bacteriophage λ. |
|---|---|
| Journal, issue, pages | Cell Rep, Vol. 45, Issue 7, Page 117691, Year 2026 |
| Publish date | Jul 17, 2026 |
Authors | Xiaofei Ge / Zhiwei Gu / Jiawei Wang / ![]() |
| PubMed Abstract | Bacteriophages face intense competition within bacterial populations. Although bacteria encode diverse anti-phage mechanisms, strategies protecting virions at the host surface remain poorly ...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. |
External links | Cell Rep / PubMed:42467530 |
| Methods | EM (single particle) |
| Resolution | 3.45 Å |
| Structure data | EMDB-66201, PDB-9wso: |
| Source |
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Keywords | VIRAL PROTEIN / membrane protein; phage protein; complex |
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escherichia phage lambda (virus)
shigella sonnei (strain ss046) (bacteria)
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