6CX1
Cryo-EM structure of Seneca Valley Virus-Anthrax Toxin Receptor 1 complex
6CX1 の概要
エントリーDOI | 10.2210/pdb6cx1/pdb |
EMDBエントリー | 7772 |
分子名称 | Anthrax toxin receptor 1, Capsid protein VP1, Capsid protein VP2, ... (5 entities in total) |
機能のキーワード | virus-receptor complex, picornavirus, senecavirus, anthrax toxin receptor, virus |
由来する生物種 | Homo sapiens (Human) 詳細 |
タンパク質・核酸の鎖数 | 5 |
化学式量合計 | 111709.36 |
構造登録者 | Jayawardena, N.,Burga, L.,Easingwood, R.,Takizawa, Y.,Wolf, M.,Bostina, M. (登録日: 2018-04-02, 公開日: 2018-10-31, 最終更新日: 2024-03-13) |
主引用文献 | Jayawardena, N.,Burga, L.N.,Easingwood, R.A.,Takizawa, Y.,Wolf, M.,Bostina, M. Structural basis for anthrax toxin receptor 1 recognition by Seneca Valley Virus. Proc. Natl. Acad. Sci. U.S.A., 115:E10934-E10940, 2018 Cited by PubMed Abstract: Recently, the use of oncolytic viruses in cancer therapy has become a realistic therapeutic option. Seneca Valley Virus (SVV) is a newly discovered picornavirus, which has earned a significant reputation as a potent oncolytic agent. Anthrax toxin receptor 1 (ANTXR1), one of the cellular receptors for the protective antigen secreted by , has been identified as the high-affinity cellular receptor for SVV. Here, we report the structure of the SVV-ANTXR1 complex determined by single-particle cryo-electron microscopy analysis at near-atomic resolution. This is an example of a shared receptor structure between a mammalian virus and a bacterial toxin. Our structure shows that ANTXR1 decorates the outer surface of the SVV capsid and interacts with the surface-exposed BC loop and loop II of VP1, "the puff" of VP2 and "the knob" of VP3. Comparison of the receptor-bound capsid structure with the native capsid structure reveals that receptor binding induces minor conformational changes in SVV capsid structure, suggesting the role of ANTXR1 as an attachment receptor. Furthermore, our results demonstrate that the capsid footprint on the receptor is not conserved in anthrax toxin receptor 2 (ANTXR2), thereby providing a molecular mechanism for explaining the exquisite selectivity of SVV for ANTXR1. PubMed: 30381454DOI: 10.1073/pnas.1810664115 主引用文献が同じPDBエントリー |
実験手法 | ELECTRON MICROSCOPY (3.8 Å) |
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