Nature Communications· 2026Q1
Proximity biotinylation at the host-Shigella interface reveals UFMylation as an antibacterial pathway
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- 2026year
Short summary
A proximity biotinylation approach mapped the host-bacterial interface during Shigella infection, revealing that the host UFMylation machinery targets intracellular bacteria.
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Key points
- Proximity biotinylation mapped host factors targeting intracellular Shigella and Salmonella.
- The host UFMylation machinery (UFL1) was identified as a key factor targeting these bacteria.
- Shigella antagonizes UFMylation via its lipopolysaccharide and the effector IpaH9.8.
- Absence of UFMylation increased bacterial burden in human cells and zebrafish.
- UFMylation functions as an antibacterial pathway independent of autophagy.
AI-generated from the title and abstract; the full text is not read.
Abstract
Abstract Host cells contest invasion by intracellular bacterial pathogens with multiple strategies that recognise and/or damage the bacterial surface. To identify host defence factors targeted to intracellular bacteria, we developed a proximity biotinylation approach coupled to quantitative mass spectrometry that maps the host-bacterial interface during infection. Using this method, we discovered that intracellular Shigella and Salmonella become targeted by UFM1-protein ligase 1 (UFL1), an E3 ligase that catalyses the covalent attachment of Ubiquitin-fold modifier 1 (UFM1) to target substrates in a process called UFMylation. Shigella antagonises UFMylation in a dual manner: first, using its lipopolysaccharide to shield from UFL1 recruitment; second, preventing UFM1 decoration by the bacterial effector IpaH9.8. Absence of UFMylation leads to an increase of bacterial burden in human cells and zebrafish larvae. Contrary to ubiquitylation, the protective role of UFMylation is independent of autophagy. Altogether, our proximity mapping of the host-bacterial interface identifies UFMylation as an ancient antibacterial pathway and holds great promise to reveal other cell-autonomous immunity mechanisms.
The authors' abstract, as published at the source. Nature Communications, 2026 · DOI ↗
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Field: Cell Biology
Cell BiologyBiochemistry, Genetics and Molecular Biology