ArticleScientific reports2018
The 2.1 Å structure of protein F9 and its comparison to L1, two components of the conserved poxvirus entry-fusion complex.
Article in Scientific reports, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed.
- Structure and functional analyses of vaccinia virus J5 protein reveal distinct determinants for entry-fusion complex assembly and activation.Journal of virology · 2026Article
- Cryo-EM structure of the vaccinia virus entry fusion complex reveals a multicomponent fusion machinery.Science advances · 2026Article
- Structural dissection of vaccinia G9 identifies residues essential for membrane fusion and complex assembly.Journal of virology · 2025Article
- The 2.3 Å Structure of A21, a Protein Component of the Conserved Poxvirus Entry-Fusion Complex.Journal of molecular biology · 2025Article
- Poxvirus structural biology for application to vaccine design.Trends in immunology · 2025Review
- Which Proteins? The Challenge of Identifying the Protective Antigens for Next-Generation Capripoxvirus Vaccines.Vaccines · 2025Review
- The evolving mpox threat (2022-2024): clade dynamics, immune evasion, and escalating global health challenges.Frontiers in cellular and infection microbiology · 2025Review
- Identification of a Potential Entry-Fusion Complex Based on Sequence Homology of African Swine Fever and Vaccinia Virus.Viruses · 2024Article
- Structural and functional analyses of viral H2 protein of the vaccinia virus entry fusion complex.Journal of virology · 2023Article
- Crystal structure of vaccinia virus G3/L5 sub-complex reveals a novel fold with extended inter-molecule interactions conserved among orthopoxviruses.Emerging microbes & infections · 2023Article
- Structural and functional analysis of vaccinia viral fusion complex component protein A28 through NMR and molecular dynamic simulations.PLoS pathogens · 2023Article
- Article
- Monkeypox: epidemiology, pathogenesis, treatment and prevention.Signal transduction and targeted therapy · 2022Review
- Characterizing and explaining the impact of disease-associated mutations in proteins without known structures or structural homologs.Briefings in bioinformatics · 2022Article
- Insights into the Organization of the Poxvirus Multicomponent Entry-Fusion Complex from Proximity Analyses in Living Infected Cells.Journal of virology · 2021Article
- Loss of the vaccinia virus 35-amino acid hydrophobic O3 protein is partially compensated by mutations in the transmembrane domains of other entry proteins.Journal of virology · 2021Article
- Article
- Mutations Near the N Terminus of Vaccinia Virus G9 Protein Overcome Restrictions on Cell Entry and Syncytium Formation Imposed by the A56/K2 Fusion Regulatory Complex.Journal of virology · 2020Article
- Experimental Evolution To Isolate Vaccinia Virus Adaptive G9 Mutants That Overcome Membrane Fusion Inhibition via the Vaccinia Virus A56/K2 Protein Complex.Journal of virology · 2020Article
- Species-Specific Conservation of Linear Antigenic Sites on Vaccinia Virus A27 Protein Homologs of Orthopoxviruses.Viruses · 2019Article
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4 authors.
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Abstract
The poxvirus F9 protein is a component of the vaccinia virus entry fusion complex (EFC) which consists of 11 proteins. The EFC forms a unique apparatus among viral fusion proteins and complexes. We solved the atomic structure of the F9 ectodomain at 2.10 Å. A structural comparison to the ectodomain of the EFC protein L1 indicated a similar fold and organization, in which a bundle of five α-helices is packed against two pairs of β-strands. However, instead of the L1 myristoylation site and hydrophobic cavity, F9 possesses a protruding loop between α-helices α3 and α4 starting at Gly90. Gly90 is conserved in all poxviruses except Salmon gill poxvirus (SGPV) and Diachasmimorpha longicaudata entomopoxvirus. Phylogenetic sequence analysis of all Poxviridae F9 and L1 orthologs revealed the SGPV genome to contain the most distantly related F9 and L1 sequences compared to the vaccinia proteins studied here. The structural differences between F9 and L1 suggest functional adaptations during evolution from a common precursor that underlie the present requirement for each protein.
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