EMD-41447
AP205 binding to one Acinetobacter GP16 type iv pilus
EMD-41447
Single-particle4.2 Å
Deposition: 03/08/2023
Map released: 06/03/2024
Last modified: 01/05/2024
Sample Organism:
Acinetobacter phage AP205
Sample: Acinetobacter phage AP205
Deposition Authors: Xing Z , Meng R , Zhang J
Sample: Acinetobacter phage AP205
Deposition Authors: Xing Z , Meng R , Zhang J
Structural basis of Acinetobacter type IV pili targeting by an RNA virus.
Meng R ,
Xing Z ,
Chang JY,
Yu Z,
Thongchol J ,
Xiao W,
Wang Y ,
Chamakura K ,
Zeng Z,
Wang F ,
Young R ,
Zeng L ,
Zhang J
(2024) Nat Commun , 15 , 2746 - 2746
(2024) Nat Commun , 15 , 2746 - 2746
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.
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.