National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)
R21AI156846
米国
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)
R01GM141659
米国
National Science Foundation (NSF, United States)
MCB-1902392
米国
Other private
Texas A&M University T3
米国
Other private
Texas A&M University X-grants
米国
Other private
Center for phage technology, TAMU
米国
National Science Foundation (NSF, United States)
PHY-1734030
米国
引用
ジャーナル: Science / 年: 2024 タイトル: Removal of type IV pili by a small RNA virus. 著者: Jirapat Thongchol / Zihao Yu / Laith Harb / Yiruo Lin / Matthias Koch / Matthew Theodore / Utkarsh Narsaria / Joshua Shaevitz / Zemer Gitai / Yinghao Wu / Junjie Zhang / Lanying Zeng / 要旨: The retractile type IV pilus (T4P) is important for virulence of the opportunistic human pathogen . The single-stranded RNA (ssRNA) phage PP7 binds to T4P and is brought to the cell surface through ...The retractile type IV pilus (T4P) is important for virulence of the opportunistic human pathogen . 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.
想定した対称性 - 点群: C1 (非対称) / 解像度のタイプ: BY AUTHOR / 解像度: 3.9 Å / 解像度の算出法: OTHER / ソフトウェア - 名称: cryoSPARC 詳細: composite map of PP7 binding to type IV pilus from PAO1, the reported resolution is from the raw map of PP7. 使用した粒子像数: 40493