ArticleScientific reports2021
High resolution cryo EM analysis of HPV16 identifies minor structural protein L2 and describes capsid flexibility.
Article in Scientific reports, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
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Who cites it
28 citing papers in PubMed, 34 citations in OpenAlex.
- Atomic resolution structure of human papillomavirus bound to heparin.Nature communications · 2026Article
- Novel avian papillomaviruses identified in a south polar skua sampled on Ross Island, Antarctica.Archives of virology · 2026Article
- Susceptibility of naturally human papillomavirus type 16 major capsid protein L1 variants to vaccines and predictions of future evolutionary trends.Tumour virus research · 2026Article
- Polyanionic Sugars Drastically Affect Assembly of Human Papilloma Virus Virus-Like Particles.ACS infectious diseases · 2026Article
- Article
- Comparative analysis of the extent of protein-protein interactions in icosahedral viral capsids.Protein science : a publication of the Protein Society · 2025Article
- Speed Matters: Directed Assembly of Icosahedral HPV Virus-Like Particles.Journal of the American Chemical Society · 2025Article
- All-atom MD simulations of the HPV16 capsid.bioRxiv : the preprint server for biology · 2025Article
- Dissociation of Macromolecules in Laser-Heated Droplets Monitored by CD-MS.Analytical chemistry · 2025Article
- Cell-Free Expression of HPV16 Minor Capsid Protein L2 and Its Interaction with S100A10.Protein and peptide letters · 2025Article
- Heterogeneity of HPV16 virus-like particles indicates a complex assembly energy surface.Virology · 2024Article
- Glycan-induced structural activation softens the human papillomavirus capsid for entry through reduction of intercapsomere flexibility.Nature communications · 2024Article
- EngineeringVaccines · 2024Review
- Infectious parvovirus B19 circulates in the blood coated with active host protease inhibitors.Nature communications · 2024Article
- Article
- AMBERff at Scale: Multimillion-Atom Simulations with AMBER Force Fields in NAMD.Journal of chemical information and modeling · 2024Article
- Article
- Sequence-independent activity of a predicted long disordered segment of the human papillomavirus type 16 L2 capsid protein during virus entry.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- A human monoclonal antibody binds within the poliovirus receptor-binding site to neutralize all three serotypes.Nature communications · 2023Article
- Cryo EM structures map a post vaccination polyclonal antibody response to canine parvovirus.Communications biology · 2023Article
Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
Human papillomavirus (HPV) is a significant health burden and leading cause of virus-induced cancers. HPV is epitheliotropic and its replication is tightly associated with terminal keratinocyte differentiation making production and purification of high titer virus preparations for research problematic, therefore alternative HPV production methods have been developed for virological and structural studies. In this study we use HPV16 quasivirus, composed of HPV16 L1/L2 capsid proteins with a packaged cottontail rabbit papillomavirus genome. We have achieved the first high resolution, 3.1 Å, structure of HPV16 by using a local subvolume refinement approach. The high resolution enabled us to build L1 unambiguously and identify L2 protein strands. The L2 density is incorporated adjacent to conserved L1 residues on the interior of the capsid. Further interpretation with our own software for Icosahedral Subvolume Extraction and Correlated Classification revealed flexibility, on the whole-particle level through diameter analysis and local movement with inter-capsomer analysis. Inter-capsomer expansion or contraction, governed by the connecting arms, showed no bias in the magnitude or direction of capsomer movement. We propose that papillomavirus capsids are dynamic and capsomers move as rigid bodies connected by flexible linkers. The resulting virus structure will provide a framework for continuing biochemical, genetic and biophysical research for papillomaviruses. Furthermore, our approach has allowed insight into the resolution barrier that has previously been a limitation in papillomavirus structural studies.
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