ArticleNature communications2023
Structural and functional analysis of the minimal orthomyxovirus-like polymerase of Tilapia Lake Virus from the highly diverged Amnoonviridae family.
Article in Nature communications, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 15 citations in OpenAlex.
- Uncovering host transcriptional responses to tilapia lake virus (TiLV) through De novo RNA-seq assembly in Nile tilapia, Oreochromis niloticus.Archives of virology · 2026Article
- Phylogenetic and Proteomic Analyses of Segment 2 Sequence Reveals the Presence of Two Variants of a Divergent Amnoonvirus (Family:Microorganisms · 2026Article
- Genome sequencing and analysis of kuchijirosho virus identify it as a novel member of the family Amnoonviridae within the order Articulavirales.Archives of virology · 2026Article
- Characterisation of the tilapia lake virus proteome and identification of an 11th protein, S9-F3.Npj viruses · 2026Article
- Exploring the Virome of Nile Tilapia (Pathogens (Basel, Switzerland) · 2025Article
- Structure of AcMNPV nucleocapsid reveals DNA portal organization and packaging apparatus of circular dsDNA baculovirus.Nature communications · 2025Article
- Structure of the tilapia lake virus nucleoprotein bound to RNA.Nucleic acids research · 2025Article
- Discovery of influenza-like virus clades in invertebrates and the evolutionary history and host-shifting events of Orthomyxoviridae in metazoans.Virus evolution · 2025Article
- biGMamAct: efficient CRISPR/Cas9-mediated docking of large functional DNA cargoes at theSynthetic biology (Oxford, England) · 2025Article
- ICTV Virus Taxonomy Profile:The Journal of general virology · 2023Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
Abstract
Tilapia Lake Virus (TiLV), a recently discovered pathogen of tilapia fish, belongs to the Amnoonviridae family from the Articulavirales order. Its ten genome segments have characteristic conserved ends and encode proteins with no known homologues, apart from the segment 1, which encodes an orthomyxo-like RNA-dependent-RNA polymerase core subunit. Here we show that segments 1-3 encode respectively the PB1, PB2 and PA-like subunits of an active heterotrimeric polymerase that maintains all domains found in the distantly related influenza polymerase, despite an unprecedented overall size reduction of 40%. Multiple high-resolution cryo-EM structures of TiLV polymerase in pre-initiation, initiation and active elongation states, show how it binds the vRNA and cRNA promoters and performs RNA synthesis, with both transcriptase and replicase configurations being characterised. However, the highly truncated endonuclease-like domain appears inactive and the putative cap-binding domain is autoinhibited, emphasising that many functional aspects of TiLV polymerase remain to be elucidated.
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