We investigated expression and localisation of all predicted proteins of Tilapia Lake Virus (TiLV) using in vitro translation, cell expression systems, and mass spectrometry, confirming major polypeptides from each segment and discovering an additional 11th protein, S9-F3, from an alternative reading frame. GFP-tagged constructs showed S2 and S10 localised mainly to the nucleus, while S1, S3, S5, S8 and S9-F3 were cytoplasmic, with S5 and S6 forming perinuclear foci. Bioinformatics and inhibitor assays revealed CRM1-dependent nuclear export of S9-F3. Evolutionary analyses indicated selective pressure on S9 and S9-F3 and identified an S9-F3 homologue in a TiLV-like guppy virus. These results reveal a novel protein and regulated nuclear export mechanism, offering new insights into TiLV biology and host interactions.
[doi:10.25345/C5XP6VG91]
[dataset license: CC0 1.0 Universal (CC0 1.0)]
Keywords: Tilapia, TiLV ; nuclear export ; accessory protein ; CRM1 ; Leptomycin B ; DatasetType:Proteomics
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Principal Investigators: (in alphabetical order) |
Paul Digard, The Roslin Institute, University of Edinburgh, United Kingdom |
| Submitting User: | domthe |
Pankaew N, Kurian D, De Angelis F, Del-Pozo J, Houston RD, Gratacap RL, Pinto RM, Digard P.
Characterisation of the tilapia lake virus proteome and identification of an 11th protein, S9-F3.
Npj Viruses. 2026 Jan 9;4(1):2. Epub 2026 Jan 9.
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