7RYJ

Cryo EM analysis reveals inherent flexibility of authentic murine papillomavirus capsids

This is a non-PDB format compatible entry.

Summary for 7RYJ

• Entry DOI: 10.2210/pdb7ryj/pdb
• EMDB information: 24741
• Descriptor: Major capsid protein L1 (1 entity in total)
• Functional Keywords: mmupv1, papillomavirus, l1, capsomer, subparticle, virus
• Biological source: Mus musculus papillomavirus type 1
• Total number of polymer chains: 6
• Total formula weight: 345741.26

Authors

Hartmann, S.R.,Hafenstein, S. (deposition date: 2021-08-25, release date: 2021-11-10, Last modification date: 2024-06-05)

Primary citation

Hartmann, S.R.,Goetschius, D.J.,Hu, J.,Graff, J.J.,Bator, C.M.,Christensen, N.D.,Hafenstein, S.L.
Cryo EM Analysis Reveals Inherent Flexibility of Authentic Murine Papillomavirus Capsids.
Viruses, 13:-, 2021

PubMed Abstract: Human papillomavirus (HPV) is a significant health burden and leading cause of virus-induced cancers. However, studies have been hampered due to restricted tropism that makes production and purification of high titer virus problematic. This issue has been overcome by developing alternative HPV production methods such as virus-like particles (VLPs), which are devoid of a native viral genome. Structural studies have been limited in resolution due to the heterogeneity, fragility, and stability of the VLP capsids. The mouse papillomavirus (MmuPV1) presented here has provided the opportunity to study a native papillomavirus in the context of a common laboratory animal. Using cryo EM to solve the structure of MmuPV1, we achieved 3.3 Å resolution with a local symmetry refinement method that defined smaller, symmetry related subparticles. The resulting high-resolution structure allowed us to build the MmuPV1 asymmetric unit for the first time and identify putative L2 density. We also used our program ISECC to quantify capsid flexibility, which revealed that capsomers move as rigid bodies connected by flexible linkers. The MmuPV1 flexibility was comparable to that of a HPV VLP previously characterized. The resulting MmuPV1 structure is a promising step forward in the study of papillomavirus and will provide a framework for continuing biochemical, genetic, and biophysical research for papillomaviruses.

PubMed: 34696452
DOI: 10.3390/v13102023

Experimental method

ELECTRON MICROSCOPY (3.3 Å)