Structural basis of Acinetobacter type IV pili targeting by an RNA virus

Ran Meng, Zhongliang Xing, Jeng-Yih Chang, Zihao Yu, Jirapat Thongchol, Wen Xiao, Yuhang Wang, Karthik Chamakura, Zhiqi Zeng, Fengbin Wang, Ry Young, Lanying Zeng and Junjie Zhang ()
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Ran Meng: Texas A&M University
Zhongliang Xing: Texas A&M University
Jeng-Yih Chang: Texas A&M University
Zihao Yu: Texas A&M University
Jirapat Thongchol: Texas A&M University
Wen Xiao: Texas A&M University
Yuhang Wang: Texas A&M University
Karthik Chamakura: Texas A&M University
Zhiqi Zeng: Texas A&M University
Fengbin Wang: University of Alabama at Birmingham
Ry Young: Texas A&M University
Lanying Zeng: Texas A&M University
Junjie Zhang: Texas A&M University

Nature Communications, 2024, vol. 15, issue 1, 1-9

Abstract: 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.

Date: 2024
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DOI: 10.1038/s41467-024-47119-5

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