A research team comprising the Faculty of Health and Wellness (FHW) at City University of Macau, Tsinghua University, and the Institute of Microbiology of the Chinese Academy of Sciences has published a paper in the top-tier journal Advanced Science (IF 15.6), titled F-Type Pyocin Versus Phage λ Tail: Conserved Hub, Divergent Fibers. The study provides the first high-resolution structural analysis of an F-type phage tail-like bacteriocin (F2-pyocin) from Pseudomonas aeruginosa, offering a clear structure for developing novel precision antibacterial therapies.
The team used cryo-electron microscopy to resolve the atomic structure of F2-pyocin. They discovered that the protein’s tail tube is composed of multiple stacked protein rings, assembled in a manner highly similar to the λ phage tail, indicating an evolutionary relationship between the two. Further analysis revealed that F2-pyocin’s lateral fibers adopt a novel anchoring mode distinct from that of the λ phage, suggesting that the protein likely achieves precision killing by recognizing specific glycan structures on the surface of Pseudomonas aeruginosa.
The corresponding authors of the paper are Associate Professor Wang Jiawei of Tsinghua University, Assistant Professor Ge Xiaofei of City University of Macau, and Researcher Ma Lüyan of the Chinese Academy of Sciences. This research was jointly funded by the Macao Science and Technology Development Fund (FDCT), the National Natural Science Foundation of China, and the Beijing Natural Science Foundation. Looking ahead, FHW will continue to focus on phage therapy and other alternatives, actively addressing the challenge of antibiotic resistance.
Source: Faculty of Health and Wellness
