Researchers have provided the first understanding of how the lipopeptide serrawettin W2-FL10, which comes from Serratia marcescens, works. This lipopeptide targets the cell membrane of S. aureus, causing damage that leads to the release of internal components and, ultimately, the death of the cell.
A new antibacterial lipopeptide made by the bacterium Serratia marcescens has been proven to be highly effective in killing Staphylococcus aureus, an important human pathogen.
Staphylococcus aureus is one of the five most common causes of hospital-acquired infections are often due to the presence of S. aureus, which can lead to life-threatening infections after surgery. Since antibiotics were first introduced in the 1940s, S. aureus has developed resistance to most types of antibiotics, including penicillin. However, only two new classes of antibiotics with unique modes of action have been introduced in the past sixty years. Daptomycin, which belongs to the lipopeptide class of antibiotics, is one of these new classes. Dr. Tanya Decker (formerly Clements) from Stellenbosch University (SU) recently published a paper in Microbiology Spectrum providing the First insight into the mechanism of action of the lipopeptide serrawettin W2-FL10, which comes from Serratia marcescens. Research has shown that this lipopeptide targets the cell membrane of S. aureus, causing damage that leads to the release of internal components and, eventually, cell death. In addition, it has been demonstrated that serrawettin W2-FL10 does not harm mammalian cells, suggesting its potential use as a treatment for bacterial infections in humans. Furthermore, the structure of this lipopeptide is much smaller than daptomycin, consisting of five amino acids and a C10 fatty acid chain compared to 13 amino acids.
One of the potential benefits of serrawettin W2-FL10 is that it contains only two amino acids and a C10 fatty acid chain, which could lower the manufacturing costs significantly.
What makes some lipopeptides effective against microbes?
Dr. Decker, a postdoctoral researcher at the Helmholtz Institute for Pharmaceutical Research Saarland in Germany, began studying serrawettin W2-FL10 in 2017 under the guidance of Prof. Wesaal Khan in SU’s Department of Microbiology. Her research built upon the work of another postgraduate student in the same group, Dr. Thando Ndlovu, who had isolated bacterial strains from wastewater samples and found their biosurfactants to be effective against microbes.Biosurfactants are naturally produced by bacteria in polluted environments to protect them from antibiotic-resistant and disease-causing bacteria. Decker’s research focused on studying the antimicrobial properties of lipopeptides derived from the bacterium Serratia. She found that both pigmented and non-pigmented S. marcescens strains produced a variety of broad-spectrum antimicrobial compounds, with the lipopeptide serrawettin W2-FL10 showing potential for further investigation.The characteristics of the research findings have been attributed to the close collaboration between Prof. Khan and Prof. Marina Rautenbach, a specialist in antimicrobial peptides, at SU’s Department of Biochemistry. Decker is also continuing her research into novel natural antimicrobial products at the Helmholtz Institute in Germany.
