ArticlePLoS pathogens2026
Transthyretin is a novel innate immune effector against Gram negative bacteria.
Article in PLoS pathogens, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
1 citing paper in PubMed.
- Encrypted immunity mediated by peptides.PLoS biology · 2026Review
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Authors and funding
8 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Pseudomonas aeruginosa is an opportunistic pathogen that frequently causes severe bloodstream and respiratory infections, yet the interactions between this bacterium and the innate immune system remain poorly investigated. In this study we identified transthyretin, the transporter protein of thyroid hormone and retinol, as a novel binding partner of the bacterium. We show that transthyretin binds to lipopolysaccharide via lipid A. Transthyretin binding induces the agglutination of transthyretin-bacteria complexes and a reduction in bacterial viability. Mapping studies reveal that the N-terminal region of transthyretin mediates bacterial interaction, and a synthetic peptide derived from this domain exhibits potent bactericidal activity against a broad collection of P. aeruginosa isolates as well as other Gram-negative bacteria by disrupting membrane integrity. These findings identify transthyretin as an endogenous antimicrobial factor and uncover cryptic antimicrobial activity within its N-terminal region. Beyond extending the functional repertoire of transthyretin, these results suggest a novel role for this protein in innate defense.
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