ArticlePLoS pathogens2016
Structure of a Spumaretrovirus Gag Central Domain Reveals an Ancient Retroviral Capsid.
Article in PLoS pathogens, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 22 citations in OpenAlex.
- Gag proteins encoded by endogenous retroviruses are required for zebrafish development.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- The Diverse Evolutionary Histories of Domesticated Metaviral Capsid Genes in Mammals.Molecular biology and evolution · 2024Article
- The diverse evolutionary histories of domesticated metaviral capsid genes in mammals.bioRxiv : the preprint server for biology · 2023Article
- Structures of the Hepaci-, Pegi-, and Pestiviruses envelope proteins suggest a novel membrane fusion mechanism.PLoS biology · 2023Article
- Structure of a Ty1 restriction factor reveals the molecular basis of transposition copy number control.Nature communications · 2021Article
- Review
- Novel Host Protein TBC1D16, a GTPase Activating Protein of Rab5C, Inhibits Prototype Foamy Virus Replication.Frontiers in immunology · 2021Article
- Structure ofScience advances · 2020Article
- The First Co-Opted Endogenous Foamy Viruses and the Evolutionary History of Reptilian Foamy Viruses.Viruses · 2019Article
- Review
- Structure of the Ty3/Gypsy retrotransposon capsid and the evolution of retroviruses.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Article
- The invariant arginine within the chromatin-binding motif regulates both nucleolar localization and chromatin binding of Foamy virus Gag.Retrovirology · 2018Article
- Homologous Capsid Proteins Testify to the Common Ancestry of Retroviruses, Caulimoviruses, Pseudoviruses, and Metaviruses.Journal of virology · 2017Article
- A comparative analysis of the foamy and ortho virus capsid structures reveals an ancient domain duplication.BMC structural biology · 2017Article
Corrections and comments
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Authors and funding
15 authors at 2 institutions in 2 countries.
Funding
Abstract
The Spumaretrovirinae, or foamy viruses (FVs) are complex retroviruses that infect many species of monkey and ape. Despite little sequence homology, FV and orthoretroviral Gag proteins perform equivalent functions, including genome packaging, virion assembly, trafficking and membrane targeting. However, there is a paucity of structural information for FVs and it is unclear how disparate FV and orthoretroviral Gag molecules share the same function. To probe the functional overlap of FV and orthoretroviral Gag we have determined the structure of a central region of Gag from the Prototype FV (PFV). The structure comprises two all α-helical domains NtDCEN and CtDCEN that although they have no sequence similarity, we show they share the same core fold as the N- (NtDCA) and C-terminal domains (CtDCA) of archetypal orthoretroviral capsid protein (CA). Moreover, structural comparisons with orthoretroviral CA align PFV NtDCEN and CtDCEN with NtDCA and CtDCA respectively. Further in vitro and functional virological assays reveal that residues making inter-domain NtDCEN-CtDCEN interactions are required for PFV capsid assembly and that intact capsid is required for PFV reverse transcription. These data provide the first information that relates the Gag proteins of Spuma and Orthoretrovirinae and suggests a common ancestor for both lineages containing an ancient CA fold.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.