In silico identification of lysocin biosynthetic gene cluster from Lysobacter sp. RH2180-5

Despite continual advances in antimicrobial therapies, infectious diseases pose a serious threat to global health owing to the ability of microbes to acquire resistance against antibiotics and transform themselves into superbugs.¹ Infectious diseases are an even more serious threat to health during immunocompromised conditions such as HIV/AIDS, diabetes and old age.² The recent increase in multidrug-resistant pathogens emphasizes the urgent need for the discovery of therapeutically active novel antimicrobial agents.¹

Lysobacter species are widely distributed in nature and characterized by their ability to lyse other organisms by producing a broad range of proteases and antibiotics.^{3, 4} Lysobacter sp. RH2180-5 was isolated from soil in Japan while screening for novel therapeutically active antibiotics using the silkworm infection model. Lysocin E, a therapeutically active novel cyclic peptide produced by Lysobacter sp. RH2180-5, has antimicrobial activity against clinical isolates of methicillin-susceptible and methicillin-resistant Staphylococcus aureus, including S. simulans, S. haemolyticus, S. pseudintermedius, Bacillus subtilis, B. cereus and Listeria monocytogenes with MICs ranging from 1–4 μg ml⁻¹.⁵ Lysocin E exhibits a novel mode of action that involves its binding to menaquinone in the cell membrane. In addition to lysocin E, Lysobacter sp. RH2180-5 produces at least eight more derivatives, most of which have antimicrobial activity. To further improve the production of lysocin E, analyze the derivatives and prepare novel derivatives with improved activity, the genetic analysis of the lysocin biosynthetic gene cluster is required.

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