期刊
SCIENCE
卷 381, 期 6654, 页码 180-+出版社
AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/science.adg9091
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In this study, the researchers used single-particle electron cryo-microscopy to uncover the mechanism by which bacteriophage can kill bacteria by encoding a protein antibiotic. The results were validated experimentally and provide a model for bacterial lysis and potential design of phage therapeutics.
The historically important phage Phi X174 kills its host bacteria by encoding a 91-residue protein antibiotic called protein E. Using single-particle electron cryo-microscopy, we demonstrate that protein E bridges two bacterial proteins to form the transmembrane YES complex [MraY, protein E, sensitivity to lysis D (SlyD)]. Protein E inhibits peptidoglycan biosynthesis by obstructing the MraY active site leading to loss of lipid I production. We experimentally validate this result for two different viral species, providing a clear model for bacterial lysis and unifying previous experimental data. Additionally, we characterize the Escherichia coli MraY structure-revealing features of this essential enzyme-and the structure of the chaperone SlyD bound to a protein. Our structures provide insights into the mechanism of phage-mediated lysis and for structure-based design of phage therapeutics.
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