6B9Q

Single particle cryo-EM structure determination of the LuIII capsid protein

This is a non-PDB format compatible entry.

Summary for 6B9Q

• Entry DOI: 10.2210/pdb6b9q/pdb
• EMDB information: 7071
• Descriptor: Capsid protein VP2 (1 entity in total)
• Functional Keywords: parvoviridae, vp2 capsid protein, virus like particle
• Biological source: Parvovirus LuIII
• Total number of polymer chains: 60
• Total formula weight: 3929397.18

Authors

Pittman, N.C.,Agbandje-McKenna, M. (deposition date: 2017-10-11, release date: 2017-11-15, Last modification date: 2025-05-21)

Primary citation

Pittman, N.,Misseldine, A.,Geilen, L.,Halder, S.,Smith, J.K.,Kurian, J.,Chipman, P.,Janssen, M.,Mckenna, R.,Baker, T.S.,D'Abramo, A.,Cotmore, S.,Tattersall, P.,Agbandje-McKenna, M.
Atomic Resolution Structure of the Oncolytic Parvovirus LuIII by Electron Microscopy and 3D Image Reconstruction.
Viruses, 9:-, 2017

PubMed Abstract: 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.

PubMed: 29084163
DOI: 10.3390/v9110321

Experimental method

ELECTRON MICROSCOPY (3.17 Å)