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

被引：2

作者：

Meng, Ran ^{[1
,3
]}

Xing, Zhongliang ^{[1
]}

Chang, Jeng-Yih ^{[1
,4
]}

Yu, Zihao ^{[1
]}

Thongchol, Jirapat ^{[1
]}

Xiao, Wen ^{[1
]}

Wang, Yuhang ^{[1
]}

Chamakura, Karthik ^{[1
,5
]}

Zeng, Zhiqi ^{[1
]}

Wang, Fengbin ^{[2
]}

Young, Ry ^{[1
]}

Zeng, Lanying ^{[1
]}

Zhang, Junjie ^{[1
]}

机构：

[1] Texas A&M Univ, Ctr Phage Technol, Dept Biochem & Biophys, College Stn, TX 77843 USA

[2] Univ Alabama Birmingham, Heersink Sch Med, Dept Biochem & Mol Genet, Birmingham, AL 35294 USA

[3] Yale Univ, New Haven, CT 06520 USA

[4] UMass Chan Med Sch, Worcester, MA 01655 USA

[5] Armata Pharmaceut Inc, Marina Del Rey, CA 90292 USA

来源：

NATURE COMMUNICATIONS | 2024年 / 15卷 / 01期

基金：

美国国家卫生研究院; 美国国家科学基金会;

关键词：

CRYO-EM STRUCTURE; MATURATION PROTEIN; CRYSTAL-STRUCTURE; VISUALIZATION; MECHANISMS; DYNAMICS; REVEALS;

D O I：

10.1038/s41467-024-47119-5

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

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.

引用

页数：9