{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Meng R"],"funding":["Foundation for the National Institutes of Health (Foundation for the National Institutes of Health, Inc.)","National Science Foundation (NSF)"],"pagination":["2746"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC10980823"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["15(1)"],"pubmed_abstract":["Acinetobacters pose a significant threat to human health, especially those with weakened immune systems. Type IV pili of acinetobacters play crucial roles in virulence and antibiotic resistance. Single-stranded RNA bacteriophages target the bacterial retractile pili, including type IV. Our study delves into the interaction between Acinetobacter phage AP205 and type IV pili. Using cryo-electron microscopy, we solve structures of the AP205 virion with an asymmetric dimer of maturation proteins, the native Acinetobacter type IV pili bearing a distinct post-translational pilin cleavage, and the pili-bound AP205 showing its maturation proteins adapted to pilin modifications, allowing each phage to bind to one or two pili. Leveraging these results, we develop a 20-kilodalton AP205-derived protein scaffold targeting type IV pili in situ, with potential for research and diagnostics."],"journal":["Nature communications"],"pubmed_title":["Structural basis of Acinetobacter type IV pili targeting by an RNA virus."],"pmcid":["PMC10980823"],"funding_grant_id":["R21AI156846","MCB-1902392","U24GM1167"],"pubmed_authors":["Chang JY","Xing Z","Chamakura K","Meng R","Zhang J","Zeng L","Zeng Z","Xiao W","Wang F","Thongchol J","Young R","Yu Z","Wang Y"],"additional_accession":[]},"is_claimable":false,"name":"Structural basis of Acinetobacter type IV pili targeting by an RNA virus.","description":"Acinetobacters pose a significant threat to human health, especially those with weakened immune systems. Type IV pili of acinetobacters play crucial roles in virulence and antibiotic resistance. Single-stranded RNA bacteriophages target the bacterial retractile pili, including type IV. Our study delves into the interaction between Acinetobacter phage AP205 and type IV pili. Using cryo-electron microscopy, we solve structures of the AP205 virion with an asymmetric dimer of maturation proteins, the native Acinetobacter type IV pili bearing a distinct post-translational pilin cleavage, and the pili-bound AP205 showing its maturation proteins adapted to pilin modifications, allowing each phage to bind to one or two pili. Leveraging these results, we develop a 20-kilodalton AP205-derived protein scaffold targeting type IV pili in situ, with potential for research and diagnostics.","dates":{"release":"2024-01-01T00:00:00Z","publication":"2024 Mar","modification":"2025-04-19T10:13:36.015Z","creation":"2025-04-19T10:13:36.015Z"},"accession":"S-EPMC10980823","cross_references":{"pubmed":["38553443"],"doi":["10.1038/s41467-024-47119-5"]}}