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TitleSeneca Valley virus attachment and uncoating mediated by its receptor anthrax toxin receptor 1.
Journal, issue, pagesProc Natl Acad Sci U S A, Vol. 115, Issue 51, Page 13087-13092, Year 2018
Publish dateDec 18, 2018
AuthorsLin Cao / Ran Zhang / Tingting Liu / Zixian Sun / Mingxu Hu / Yuna Sun / Lingpeng Cheng / Yu Guo / Sheng Fu / Junjie Hu / Xiangmin Li / Chengqi Yu / Hanyang Wang / Huanchun Chen / Xueming Li / Elizabeth E Fry / David I Stuart / Ping Qian / Zhiyong Lou / Zihe Rao /
PubMed AbstractSeneca Valley virus (SVV) is an oncolytic picornavirus with selective tropism for neuroendocrine cancers. SVV mediates cell entry by attachment to the receptor anthrax toxin receptor 1 (ANTXR1). Here ...Seneca Valley virus (SVV) is an oncolytic picornavirus with selective tropism for neuroendocrine cancers. SVV mediates cell entry by attachment to the receptor anthrax toxin receptor 1 (ANTXR1). Here we determine atomic structures of mature SVV particles alone and in complex with ANTXR1 in both neutral and acidic conditions, as well as empty "spent" particles in complex with ANTXR1 in acidic conditions by cryoelectron microscopy. SVV engages ANTXR1 mainly by the VP2 DF and VP1 CD loops, leading to structural changes in the VP1 GH loop and VP3 GH loop, which attenuate interprotomer interactions and destabilize the capsid assembly. Despite lying on the edge of the attachment site, VP2 D146 interacts with the metal ion in ANTXR1 and is required for cell entry. Though the individual substitution of most interacting residues abolishes receptor binding and virus propagation, a serine-to-alanine mutation at VP2 S177 significantly increases SVV proliferation. Acidification of the SVV-ANTXR1 complex results in a major reconfiguration of the pentameric capsid assemblies, which rotate ∼20° around the icosahedral fivefold axes to form a previously uncharacterized spent particle resembling a potential uncoating intermediate with remarkable perforations at both two- and threefold axes. These structures provide high-resolution snapshots of SVV entry, highlighting opportunities for anticancer therapeutic optimization.
External linksProc Natl Acad Sci U S A / PubMed:30514821 / PubMed Central
MethodsEM (single particle)
Resolution2.84 - 3.38 Å
Structure data

9607

6adl

EMDB-9607, PDB-6adl:
Anthrax Toxin Receptor 1-bound spent particles of Seneca Valley Virus in acidic conditions
Method: EM (single particle) / Resolution: 3.08 Å

9608

6adm

EMDB-9608, PDB-6adm:
Anthrax Toxin Receptor 1-bound full particles of Seneca Valley Virus in acidic conditions
Method: EM (single particle) / Resolution: 2.84 Å

9611

6adr

EMDB-9611, PDB-6adr:
Anthrax Toxin Receptor 1-bound the Seneca Valley Virus in neutral conditions
Method: EM (single particle) / Resolution: 3.38 Å

9612

6ads

EMDB-9612, PDB-6ads:
Structure of Seneca Valley Virus in acidic conditions
Method: EM (single particle) / Resolution: 2.84 Å

9613

6adt

EMDB-9613, PDB-6adt:
Structure of Seneca Valley Virus in neutral condition
Method: EM (single particle) / Resolution: 3.22 Å

Chemicals

ChemComp-MG:
Unknown entry

ChemComp-HOH:
WATER

Source
  • senecavirus a
  • homo sapiens (human)
  • seneca valley virus
KeywordsVIRUS / Seneca Valley virus

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