6CX1

Cryo-EM structure of Seneca Valley Virus-Anthrax Toxin Receptor 1 complex

Summary for 6CX1

• Entry DOI: 10.2210/pdb6cx1/pdb
• EMDB information: 7772
• Descriptor: Anthrax toxin receptor 1, Capsid protein VP1, Capsid protein VP2, ... (5 entities in total)
• Functional Keywords: virus-receptor complex, picornavirus, senecavirus, anthrax toxin receptor, virus
• Biological source: Homo sapiens (Human); More
• Total number of polymer chains: 5
• Total formula weight: 111709.36

Authors

Jayawardena, N.,Burga, L.,Easingwood, R.,Takizawa, Y.,Wolf, M.,Bostina, M. (deposition date: 2018-04-02, release date: 2018-10-31, Last modification date: 2024-03-13)

Primary citation

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

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: 30381454
DOI: 10.1073/pnas.1810664115

Experimental method

ELECTRON MICROSCOPY (3.8 Å)