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dc.contributor.authorHassan, Sidra
dc.contributor.authorSyun-ichi, Urayama
dc.contributor.authorShabeer, Saba
dc.contributor.authorKiran, Tahseen Ali
dc.contributor.authorWu, Chien-Fu
dc.contributor.authorMoriyama, Hiromitsu
dc.contributor.authorCoutts, Robert H.A.
dc.contributor.authorKotta Loizou, Ioly
dc.contributor.authorJamal, Atif
dc.date.accessioned2024-03-25T13:34:11Z
dc.date.available2024-03-25T13:34:11Z
dc.date.issued2024-05
dc.identifier.citationHassan , S , Syun-ichi , U , Shabeer , S , Kiran , T A , Wu , C-F , Moriyama , H , Coutts , R H A , Kotta Loizou , I & Jamal , A 2024 , ' Molecular and biological characterization of a novel partitivirus from Talaromyces pinophilus ' , Virus Research , vol. 343 , 199351 , pp. 1-10 . https://doi.org/10.1016/j.virusres.2024.199351
dc.identifier.issn0168-1702
dc.identifier.otherJisc: 1827134
dc.identifier.otherORCID: /0000-0003-3277-6359/work/155559528
dc.identifier.urihttp://hdl.handle.net/2299/27648
dc.description© 2024 The Author(s). Published by Elsevier B.V. This is an open access article distributed under the terms of the Creative Commons Attribution License (CC BY), https://creativecommons.org/licenses/by/4.0/
dc.description.abstractTalaromyces spp. have a worldwide distribution, are ecologically diverse and have been isolated from numerous different substrates. Talaromyces spp. are considered biotechnologically important due to their ability to produce a range of enzymes and pigments. Talaromyces pinophilus, belonging to genus Talaromyces and family Trichocomaceae, is known for producing several important bioactive metabolites. Here we report the isolation and characterisation of a partitivirus from T. pinophilus which we have nominated Talaromyces pinophilus partitivirus-1 (TpPV-1). TpPV-1 possesses a genome consisting of three double stranded (ds) RNA segments i.e., dsRNAs1-3, 1824 bp, 1638 bp and 1451 bp respectively, which are encapsidated in icosahedral particles 35 nm in diameter. Both dsRNA1 and dsRNA2 contain a single open reading frame (ORF) encoding respectively a 572 amino acid (aa) protein of 65 kDa and a 504 aa protein of 50 kDa. The third segment (dsRNA3) is potentially a satellite RNA. Phylogenetic analysis revealed that the TpPV-1 belongs to the family Partitiviridae in the proposed genus Zetapartitivirus. TpPV-1 infection decreases the mycelial growth rate of the host fungus and alters pigmentation as indicated by time course experiments performed on a range of different solid media comparing virus-infected and virus-free isogenic lines. This is the first report of mycovirus infection in T. pinophilus and may provide insights into understanding the effect of the mycovirus on the production of enzymes and pigments by the host fungus.en
dc.format.extent10
dc.format.extent9644217
dc.language.isoeng
dc.relation.ispartofVirus Research
dc.subjectDouble-stranded RNA
dc.subjectGrowth
dc.subjectMetabolism
dc.subjectPartitiviridae
dc.subjectPigmentation
dc.subjectSatellite RNA
dc.subjectTalaromyces pinophilus
dc.subjectZetapartitivirus
dc.subjectInfectious Diseases
dc.subjectCancer Research
dc.subjectVirology
dc.titleMolecular and biological characterization of a novel partitivirus from Talaromyces pinophilusen
dc.contributor.institutionDepartment of Clinical, Pharmaceutical and Biological Science
dc.contributor.institutionCentre for Agriculture, Food and Environmental Management Research
dc.contributor.institutionSchool of Life and Medical Sciences
dc.contributor.institutionCrop Protection and Climate Change
dc.contributor.institutionAgriculture, Food and Veterinary Sciences
dc.description.statusPeer reviewed
dc.identifier.urlhttp://www.scopus.com/inward/record.url?scp=85187531769&partnerID=8YFLogxK
rioxxterms.versionofrecord10.1016/j.virusres.2024.199351
rioxxterms.typeJournal Article/Review
herts.preservation.rarelyaccessedtrue


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