8tux
Capsid of mature PP7 virion with 3'end region of PP7 genomic RNACapsid of mature PP7 virion with 3'end region of PP7 genomic RNA
Structural highlights
FunctionMATA_BPPP7 The maturation protein is required for the typical attachment of the phage to the side of the bacterial F-pili. Binds to sequences located toward each end of the genome, hence circularizing it. The RNA genome-maturation protein A complex is released from the capsid upon host receptor binding. Maturation protein A enters the cell along with the viral RNA.[UniProtKB:P03610] Publication Abstract from PubMedThe retractile type IV pilus (T4P) is important for virulence of the opportunistic human pathogen Pseudomonas aeruginosa. The single-stranded RNA (ssRNA) phage PP7 binds to T4P and is brought to the cell surface through pilus retraction. Using fluorescence microscopy, we discovered that PP7 detaches T4P, which impairs cell motility and restricts the pathogen's virulence. Using cryo-electron microscopy, mutagenesis, optical trapping, and Langevin dynamics simulation, we resolved the structure of PP7, T4P, and the PP7/T4P complex and showed that T4P detachment is driven by the affinity between the phage maturation protein and its bound pilin, plus the pilus retraction force and speed, and pilus bending. Pilus detachment may be widespread among other ssRNA phages and their retractile pilus systems and offers new prospects for antibacterial prophylaxis and therapeutics. Removal of Pseudomonas type IV pili by a small RNA virus.,Thongchol J, Yu Z, Harb L, Lin Y, Koch M, Theodore M, Narsaria U, Shaevitz J, Gitai Z, Wu Y, Zhang J, Zeng L Science. 2024 Apr 5;384(6691):eadl0635. doi: 10.1126/science.adl0635. Epub 2024 , Apr 5. PMID:38574145[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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