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dc.contributor.authorKannimuthu, Dhamotharan
dc.contributor.authorVendramin, Niccolò
dc.contributor.authorMarkussen, Turhan
dc.contributor.authorWessel, Øystein
dc.contributor.authorCuenca, Argelia
dc.contributor.authorNyman, Ingvild Berg
dc.contributor.authorOlsen, Anne Berit
dc.contributor.authorTengs, Torstein
dc.contributor.authorDahle, Maria
dc.contributor.authorRimstad, Espen
dc.date.accessioned2018-10-25T10:59:51Z
dc.date.available2018-10-25T10:59:51Z
dc.date.created2018-05-12T13:34:09Z
dc.date.issued2018
dc.identifier.citationViruses. 2018, 10 (4), 1-16.nb_NO
dc.identifier.issn1999-4915
dc.identifier.urihttp://hdl.handle.net/11250/2569552
dc.description.abstractPiscine 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.
dc.description.abstractMolecular and antigenic characterization of piscine orthoreovirus (PRV) from rainbow trout (oncorhynchus orthoreovirumykiss)
dc.language.isoengnb_NO
dc.relation.urihttp://www.mdpi.com/1999-4915/10/4/170/htm
dc.rightsAttribution-NonCommercial-NoDerivatives 4.0 Internasjonal*
dc.rights.urihttp://creativecommons.org/licenses/by-nc-nd/4.0/deed.no*
dc.titleMolecular and antigenic characterization of piscine orthoreovirus (PRV) from rainbow trout (oncorhynchus orthoreovirumykiss)nb_NO
dc.title.alternativeMolecular and antigenic characterization of piscine orthoreovirus (PRV) from rainbow trout (oncorhynchus orthoreovirumykiss)nb_NO
dc.typeJournal articlenb_NO
dc.typePeer reviewednb_NO
dc.description.versionpublishedVersion
dc.source.pagenumber1-16nb_NO
dc.source.volume10nb_NO
dc.source.journalVirusesnb_NO
dc.source.issue4nb_NO
dc.identifier.doi10.3390/v10040170
dc.identifier.cristin1584680
dc.relation.projectNorges forskningsråd: 237315/E40nb_NO
cristin.unitcode192,16,2,0
cristin.unitcode192,12,0,0
cristin.unitnameInstitutt for mattrygghet og infeksjonsbiologi
cristin.unitnameKjemi, bioteknologi og matvitenskap
cristin.ispublishedtrue
cristin.fulltextoriginal
cristin.qualitycode1


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Attribution-NonCommercial-NoDerivatives 4.0 Internasjonal
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