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TitleStructural basis for anthrax toxin receptor 1 recognition by Seneca Valley Virus.
Journal, issue, pagesProc Natl Acad Sci U S A, Vol. 115, Issue 46, Page E10934-E10940, Year 2018
Publish dateNov 13, 2018
AuthorsNadishka Jayawardena / Laura N Burga / Richard A Easingwood / Yoshimasa Takizawa / Matthias Wolf / Mihnea Bostina /
PubMed AbstractRecently, 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 ...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.
External linksProc Natl Acad Sci U S A / PubMed:30381454 / PubMed Central
MethodsEM (single particle)
Resolution3.8 Å
Structure data

EMDB-7772, PDB-6cx1:
Cryo-EM structure of Seneca Valley Virus-Anthrax Toxin Receptor 1 complex
Method: EM (single particle) / Resolution: 3.8 Å

Source
  • homo sapiens (human)
  • senecavirus a
KeywordsVIRUS / Virus-receptor complex / Picornavirus / Senecavirus / Anthrax Toxin Receptor

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