A novel Flavobacterium quisquiliarum porphyrin binding protein independently disrupts Pseudomonas aeruginosa biofilms

Authors: Ieva Lelenaite, Charlotte Stenkjær Fletcher, William Houppy et al.

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Published: Unknown date

Source: Crossref

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Abstract

<title>Abstract</title> <p> Bacterial biofilms underpin chronic infection and antimicrobial resistance, notably in <italic>Pseudomonas aeruginosa</italic> . Here we deconvolute a commercial alginate lyase preparation from <italic>Flavobacterium quisquiliarum</italic> and identify a previously uncharacterised ~ 21 kDa porphyrin-binding protein ( <italic>Fq</italic> PBP). Structural, biophysical and docking analyses reveal high-affinity tetrapyrrole binding. Recombinant <italic>Fq</italic> PBP independently inhibits and disperses <italic>P. aeruginosa</italic> biofilms, implicating porphyrin sequestration and iron homeostasis in biofilm control and highlighting a potential therapeutic strategy targeting iron acquisition pathways. Data are available via ProteomeXchange with identifier PXD081358. </p>

Keywords

biofilms aeruginosa iron abstract bacterial

A novel Flavobacterium quisquiliarum porphyrin binding protein independently disrupts Pseudomonas aeruginosa biofilms

Abstract

Keywords

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