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-Structure paper
タイトル | Structural basis of Acinetobacter type IV pili targeting by an RNA virus. |
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ジャーナル・号・ページ | Nat Commun, Vol. 15, Issue 1, Page 2746, Year 2024 |
掲載日 | 2024年3月29日 |
著者 | 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 / Junjie Zhang / |
PubMed 要旨 | 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. ...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. |
リンク | Nat Commun / PubMed:38553443 / PubMed Central |
手法 | EM (らせん対称) / EM (単粒子) |
解像度 | 3.0 - 8.55 Å |
構造データ | EMDB-41442, PDB-8tob: EMDB-41443, PDB-8toc: EMDB-41447: AP205 binding to one Acinetobacter GP16 type iv pilus EMDB-41634, PDB-8tv9: EMDB-41635, PDB-8tva: EMDB-41646: AP205 phage Acinetobacter gp16 T4P complex EMDB-41657, PDB-8tw2: EMDB-41666, PDB-8twc: |
由来 |
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キーワード | CELL ADHESION / T4P / Competence / VIRUS/RNA / Acinetobacter / SsRNA phage virus / VIRUS / VIRUS-RNA complex / VIRUS LIKE PARTICLE / VLP |