EMD-41666
Acinetobacter phage AP205 T=3 VLP
EMD-41666
Single-particle3.0 Å
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Map released: 06/03/2024
Last modified: 09/10/2024
Sample Organism:
Acinetobacter phage AP205
Sample: Acinetobacter phage AP205
Fitted models: 8twc (Avg. Q-score: 0.46)
Deposition Authors: Meng R
,
Xing Z
,
Zhang J
,
Zhang J
Sample: Acinetobacter phage AP205
Fitted models: 8twc (Avg. Q-score: 0.46)
Deposition Authors: Meng R
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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
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(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.