Removal of Pseudomonas type IV pili by a small RNA virus

被引:4
|
作者
Thongchol, Jirapat [1 ,2 ]
Yu, Zihao [1 ,2 ]
Harb, Laith [1 ,2 ]
Lin, Yiruo [3 ]
Koch, Matthias [4 ,5 ,6 ,7 ]
Theodore, Matthew [1 ,2 ]
Narsaria, Utkarsh [1 ,2 ]
Shaevitz, Joshua [4 ,6 ]
Gitai, Zemer [5 ]
Wu, Yinghao [8 ]
Zhang, Junjie [1 ,2 ]
Zeng, Lanying [1 ,2 ]
机构
[1] Texas A&M Univ, Dept Biochem & Biophys, College Stn, TX 77843 USA
[2] Texas A&M Univ, Ctr Phage Technol, College Stn, TX 77843 USA
[3] Texas A&M Univ, Dept Comp Sci & Engn, College Stn, TX 77843 USA
[4] Princeton Univ, Lewis Sigler Inst Integrat Genom, Princeton, NJ 08544 USA
[5] Princeton Univ, Dept Mol Biol, Princeton, NJ 08544 USA
[6] Princeton Univ, Joseph Henry Labs Phys, Princeton, NJ 08544 USA
[7] Texas A&M Univ, Dept Biol, College Stn, TX 77843 USA
[8] Albert Einstein Coll Med, Dept Syst & Computat Biol, Bronx, NY 10461 USA
基金
美国国家科学基金会; 美国国家卫生研究院;
关键词
CRYO-EM STRUCTURE; TWITCHING MOTILITY; PROTEIN; AERUGINOSA; PLATFORM; REVEALS; GENOME;
D O I
10.1126/science.adl0635
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
The retractile type IV pilus (T4P) is important for virulence of the opportunistic human pathogen Pseudomonas aeruginosa. The single-stranded RNA (ssRNA) phage PP7 binds to T4P and is brought to the cell surface through pilus retraction. Using fluorescence microscopy, we discovered that PP7 detaches T4P, which impairs cell motility and restricts the pathogen's virulence. Using cryo-electron microscopy, mutagenesis, optical trapping, and Langevin dynamics simulation, we resolved the structure of PP7, T4P, and the PP7/T4P complex and showed that T4P detachment is driven by the affinity between the phage maturation protein and its bound pilin, plus the pilus retraction force and speed, and pilus bending. Pilus detachment may be widespread among other ssRNA phages and their retractile pilus systems and offers new prospects for antibacterial prophylaxis and therapeutics.
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页数:11
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