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