{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Hartmann SR"],"funding":["NIH Office of the Director","NIAID NIH HHS","J. Gotten Memorial Gold Tournament","Pennsylvania Department of Health","NIH HHS"],"pagination":["2023"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC8537154"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["13(10)"],"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 defin"],"journal":["Viruses"],"pubmed_title":["Cryo EM Analysis Reveals Inherent Flexibility of Authentic Murine Papillomavirus Capsids."],"pmcid":["PMC8537154"],"funding_grant_id":["no number","R01 AI134910","S10 OD026822-01","S10 OD026822","Al134910-01A1"],"pubmed_authors":["Hafenstein SL","Christensen ND","Hartmann SR","Hu J","Graff JJ","Goetschius DJ","Bator CM"],"additional_accession":[]},"is_claimable":false,"name":"Cryo EM Analysis Reveals Inherent Flexibility of Authentic Murine Papillomavirus Capsids.","description":"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 defin","dates":{"release":"2021-01-01T00:00:00Z","publication":"2021 Oct","modification":"2026-04-08T07:02:53.055Z","creation":"2025-04-06T23:24:23.586Z"},"accession":"S-EPMC8537154","cross_references":{"pubmed":["34696452"],"doi":["10.3390/v13102023"]}}