Structural basis of Acinetobacter type IV pili targeting by an RNA virus. Academic Article uri icon

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.

published proceedings

  • Nat Commun

author list (cited authors)

  • Meng, R., Xing, Z., Chang, J., Yu, Z., Thongchol, J., Xiao, W., ... Zhang, J.

complete list of authors

  • Meng, Ran||Xing, Zhongliang||Chang, Jeng-Yih||Yu, Zihao||Thongchol, Jirapat||Xiao, Wen||Wang, Yuhang||Chamakura, Karthik||Zeng, Zhiqi||Wang, Fengbin||Young, Ry||Zeng, Lanying||Zhang, Junjie

publication date

  • March 2024