ArticleCurrent microbiology2026
Mining Microbial Genomes for Anti-Pseudomonal Peptides: A Translational In Silico Framework.
Article in Current microbiology, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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Abstract
Pseudomonas aeruginosa constitutes a substantial health risk, instigating diseases such as pneumonia and sepsis in vulnerable hospitalized patients. The World Health Organization categorizes it as a high-priority bacterial pathogen owing to its marked resistance to multiple antibiotics. This pathogen poses substantial management challenges, thereby necessitating the exploration of alternative therapeutic strategies. Computational methodologies facilitate the rapid identification of antimicrobial peptides (AMPs) with heightened specificity and effectiveness against P. aeruginosa by employing genomic, transcriptomic, and structural data. This in silico study aims to identify AMPs from Bacillus and Pseudomonas genomes that may act against multidrug-resistant (MDR) P. aeruginosa by targeting Pyocyanin (PYC, a pigment virulence factor) and key membrane lipids. From 500 AMPs analyzed in the 351 genomes of Bacillus and Pseudomonas, three noteworthy candidates were identified: UviB from Bacillus altitudinis, along with two Colicins from P. koreensis and P. monsensis. The Colicins surpassed UviB in all evaluations, being nontoxic, nonhemolytic, nonallergic, biofilm-active, highly stable, and immunogenic, thus encouraging further investigation. The Colicin from P. koreensis (ColicinPk) exhibited significant non-bonded interactions with PYC, maintaining persistent proximity throughout the simulations. Both ColicinPk and ColicinPm (from P. monsensis) encompassed the pathogen’s primary lipids, Phosphatidylglycerol (PGL) and Phosphatidylethanolamine (PEA), respectively. The separation of ColicinPk from PGL was dynamically constrained via transient hydrogen bonds and non-bonded interactions. ColicinPm-PEA also showed an attractive free energy landscape like ColicinPk-PYC. Hence, these Colicins might counteract MDR P. aeruginosa by neutralizing PYC and damaging its membrane structure through interactions with key lipid backbones.
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