Molecular and Antigenic Characterization of Piscine orthoreovirus (PRV) from Rainbow Trout (Oncorhynchus mykiss)

• Published in: Viruses
• Main Authors: Kannimuthu Dhamotharan, Niccolò Vendramin, Turhan Markussen, Øystein Wessel, Argelia Cuenca, Ingvild B. Nyman, Anne Berit Olsen, Torstein Tengs, Maria Krudtaa Dahle, Espen Rimstad
• Format: Article in Journal/Newspaper
• Language: English
• Published: MDPI AG 2018
• Subjects: Piscine orthoreovirus; heart- and skeletal muscle inflammation; PRV-3; rainbow trout; Microbiology; QR1-502; Norway; Atlantic salmon; Salmo salar
• Online Access: https://doi.org/10.3390/v10040170; https://doaj.org/article/96ff6d2dad4548dabe2e965926577941

Piscine orthoreovirus (PRV-1) causes heart and skeletal muscle inflammation (HSMI) in farmed Atlantic salmon (Salmo salar). Recently, a novel PRV (formerly PRV-Om, here called PRV-3), was found in rainbow trout (Oncorhynchus mykiss) with HSMI-like disease. PRV is considered to be an emerging pathogen in farmed salmonids. In this study, molecular and antigenic characterization of PRV-3 was performed. Erythrocytes are the main target cells for PRV, and blood samples that were collected from experimentally challenged fish were used as source of virus. Virus particles were purified by gradient ultracentrifugation and the complete coding sequences of PRV-3 were obtained by Illumina sequencing. When compared to PRV-1, the nucleotide identity of the coding regions was 80.1%, and the amino acid identities of the predicted PRV-3 proteins varied from 96.7% (λ1) to 79.1% (σ3). Phylogenetic analysis showed that PRV-3 belongs to a separate cluster. The region encoding σ3 were sequenced from PRV-3 isolates collected from rainbow trout in Europe. These sequences clustered together, but were distant from PRV-3 that was isolated from rainbow trout in Norway. Bioinformatic analyses of PRV-3 proteins revealed that predicted secondary structures and functional domains were conserved between PRV-3 and PRV-1. Rabbit antisera raised against purified virus or various recombinant virus proteins from PRV-1 all cross-reacted with PRV-3. Our findings indicate that despite different species preferences of the PRV subtypes, several genetic, antigenic, and structural properties are conserved between PRV-1 and-3.