CYP168A1 from Pseudomonas aeruginosa may not be involved in the hydroxylation of medium chain-length fatty acids

Pseudomonas aeruginosa is a Gram-negative opportunistic pathogen and the main cause of chronic lung infections in patients with cystic fibrosis (CF). Its resistance to multiple antibiotics poses a significant challenge in eradicating the bacteria from CF’s patients airways. Consequently, the World Health Organization (WHO) has classified it as priority health concern, underscoring the urgent need to identify new antibiotic targets. While the function of cytochrome P450 (P450) enzymes in P. aeruginosa remains unclear, these enzymes are involved in fatty acid metabolism in Mycobacterium tuberculosis, a closely related bacterium, aiding its survival and growth in the lung. This suggests that P. aeruginosa P450 enzymes might contribute to CF airway colonization and the lung destruction by hydroxylating fatty acids in the lung surfactant. Previous research has demonstrated that CYP168A1, a P450 enzyme in P. aeruginosa, can biochemically hydroxylate fatty acids. To explore the biological role of CYP168A1, we monitored changes in gene expression after fatty acids exposure using RT-PCR. Our analyses revealed no change in CYP168A1 expression, suggesting that CYP168A1 is not involved in hydroxylation of medium-chain length fatty acids. Further knock-out analyses are essential to elucidate the biological role of CYP168A1, and its potential as an antimicrobial target against P. aeruginosa.