bioRxiv · 10.64898/2026.04.07.716877
A novel Flavobacterium quisquiliarum porphyrin binding protein independently disrupts Pseudomonas aeruginosa biofilms
Abstract
Bacterial biofilms underpin chronic infection and antimicrobial resistance, notably in Pseudomonas aeruginosa. Here we deconvolute a commercial alginate lyase preparation from Flavobacterium quisquiliarum and identify a previously uncharacterised [~]21 kDa porphyrin-binding protein (FqPBP). Structural, biophysical and docking analyses reveal high-affinity tetrapyrrole binding. Recombinant FqPBP independently inhibits and disperses P. aeruginosa biofilms, implicating porphyrin sequestration and iron homeostasis in biofilm control and highlighting a potential therapeutic strategy targeting iron acquisition pathways.
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Lelenaite, I., Fletcher, C. S., Houppy, W., Morley, C., Brown, A., Black, G. W., Malekpour, A. K., Brown, N. L., Singh, W., Munoz, J., Yau, H. C. L., Lant, N., Willats, W.. 2026-04-07. A novel Flavobacterium quisquiliarum porphyrin binding protein independently disrupts Pseudomonas aeruginosa biofilms. https://doi.org/10.64898/2026.04.07.716877
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