biostudies-literatureMeng RFoundation for the National Institutes of Health (Foundation for the National Institutes of Health, Inc.)National Science Foundation (NSF)2746https://www.ebi.ac.uk/biostudies/studies/S-EPMC10980823biostudies-literatureUnknown15(1)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.Nature communicationsStructural basis of Acinetobacter type IV pili targeting by an RNA virus.PMC10980823R21AI156846MCB-1902392U24GM1167Chang JYXing ZChamakura KMeng RZhang JZeng LZeng ZXiao WWang FThongchol JYoung RYu ZWang YfalseStructural basis of Acinetobacter type IV pili targeting by an RNA virus.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.2024-01-01T00:00:00Z2024 Mar2025-04-19T10:13:36.015Z2025-04-19T10:13:36.015ZS-EPMC109808233855344310.1038/s41467-024-47119-5