9WSO

LamB binding with bacteriophage Lom

This is a non-PDB format compatible entry.

Summary for 9WSO

• Entry DOI: 10.2210/pdb9wso/pdb
• EMDB information: 66201
• Descriptor: Maltoporin, Outer membrane protein lom (2 entities in total)
• Functional Keywords: membrane protein; phage protein; complex, viral protein
• Biological source: Shigella sonnei (strain Ss046); More
• Total number of polymer chains: 5
• Total formula weight: 186463.48

Authors

Ge, X.F.,Wang, J.W. (deposition date: 2025-09-14, release date: 2026-07-01, Last modification date: 2026-07-29)

Primary citation

Ge, X.,Gu, Z.,Wang, J.
A receptor-centered approach identifies Lom as a LamB-bound superinfection exclusion factor in bacteriophage lambda.
Cell Rep, 45:117691-117691, 2026

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 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.

PubMed: 42467530
DOI: 10.1016/j.celrep.2026.117691

Experimental method

ELECTRON MICROSCOPY (3.45 Å)