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TitleAtomic Resolution Structure of the Oncolytic Parvovirus LuIII by Electron Microscopy and 3D Image Reconstruction.
Journal, issue, pagesViruses, Vol. 9, Issue 11, Year 2017
Publish dateOct 30, 2017
AuthorsNikéa Pittman / Adam Misseldine / Lorena Geilen / Sujata Halder / J Kennon Smith / Justin Kurian / Paul Chipman / Mandy Janssen / Robert Mckenna / Timothy S Baker / Anthony D'Abramo / Susan Cotmore / Peter Tattersall / Mavis Agbandje-McKenna /
PubMed AbstractLuIII, a protoparvovirus pathogenic to rodents, replicates in human mitotic cells, making it applicable for use to kill cancer cells. This virus group includes H-1 parvovirus (H-1PV) and minute virus ...LuIII, a protoparvovirus pathogenic to rodents, replicates in human mitotic cells, making it applicable for use to kill cancer cells. This virus group includes H-1 parvovirus (H-1PV) and minute virus of mice (MVM). However, LuIII displays enhanced oncolysis compared to H-1PV and MVM, a phenotype mapped to the major capsid viral protein 2 (VP2). This suggests that within LuIII VP2 are determinants for improved tumor lysis. To investigate this, the structure of the LuIII virus-like-particle was determined using single particle cryo-electron microscopy and image reconstruction to 3.17 Å resolution, and compared to the H-1PV and MVM structures. The LuIII VP2 structure, ordered from residue 37 to 587 (C-terminal), had the conserved VP topology and capsid morphology previously reported for other protoparvoviruses. This includes a core β-barrel and α-helix A, a depression at the icosahedral 2-fold and surrounding the 5-fold axes, and a single protrusion at the 3-fold axes. Comparative analysis identified surface loop differences among LuIII, H-1PV, and MVM at or close to the capsid 2- and 5-fold symmetry axes, and the shoulder of the 3-fold protrusions. The 2-fold differences cluster near the previously identified MVM sialic acid receptor binding pocket, and revealed potential determinants of protoparvovirus tumor tropism.
External linksViruses / PubMed:29084163 / PubMed Central
MethodsEM (single particle)
Resolution3.17 Å
Structure data

7071

6b9q

EMDB-7071, PDB-6b9q:
Single particle cryo-EM structure determination of the LuIII capsid protein
Method: EM (single particle) / Resolution: 3.17 Å

Source
  • parvovirus luiii
KeywordsVIRUS LIKE PARTICLE / Parvoviridae / VP2 capsid protein

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