<?xml version="1.0" encoding="UTF-8"?><?xml-stylesheet type="text/xsl" href="static/style.xsl"?><OAI-PMH xmlns="http://www.openarchives.org/OAI/2.0/" xmlns:xsi="http://www.w3.org/2001/XMLSchema-instance" xsi:schemaLocation="http://www.openarchives.org/OAI/2.0/ http://www.openarchives.org/OAI/2.0/OAI-PMH.xsd"><responseDate>2026-07-21T14:26:56Z</responseDate><request verb="GetRecord" identifier="oai:repisalud.isciii.es:20.500.12105/6619" metadataPrefix="marc">https://repisalud.isciii.es/rest/oai/request</request><GetRecord><record><header><identifier>oai:repisalud.isciii.es:20.500.12105/6619</identifier><datestamp>2024-09-27T20:18:44Z</datestamp><setSpec>com_20.500.12105_2052</setSpec><setSpec>com_20.500.12105_2051</setSpec><setSpec>col_20.500.12105_19609</setSpec></header><metadata><record xmlns="http://www.loc.gov/MARC21/slim" xmlns:dcterms="http://purl.org/dc/terms/" xmlns:doc="http://www.lyncode.com/xoai" xmlns:xsi="http://www.w3.org/2001/XMLSchema-instance" xsi:schemaLocation="http://www.loc.gov/MARC21/slim http://www.loc.gov/standards/marcxml/schema/MARC21slim.xsd">
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      <subfield code="a">Mata, Carlos P</subfield>
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      <subfield code="a">Luque, Daniel</subfield>
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      <subfield code="a">Gómez-Blanco, Josué</subfield>
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      <subfield code="a">Rodriguez Martinez, Javier M</subfield>
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      <subfield code="a">González, José M</subfield>
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      <subfield code="a">Suzuki, Nobuhiro</subfield>
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      <subfield code="a">Ghabrial, Said A</subfield>
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      <subfield code="a">Carrascosa, José L</subfield>
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      <subfield code="a">Trus, Benes L</subfield>
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      <subfield code="a">Castón, José R</subfield>
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      <subfield code="c">2017-12-08</subfield>
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      <subfield code="a">Unlike their counterparts in bacterial and higher eukaryotic hosts, most fungal viruses are transmitted intracellularly and lack an extracellular phase. Here we determined the cryo-EM structure at 3.7 Å resolution of Rosellinia necatrix quadrivirus 1 (RnQV1), a fungal double-stranded (ds)RNA virus. RnQV1, the type species of the family Quadriviridae, has a multipartite genome consisting of four monocistronic segments. Whereas most dsRNA virus capsids are based on dimers of a single protein, the ~450-Å-diameter, T = 1 RnQV1 capsid is built of P2 and P4 protein heterodimers, each with more than 1000 residues. Despite a lack of sequence similarity between the two proteins, they have a similar α-helical domain, the structural signature shared with the lineage of the dsRNA bluetongue virus-like viruses. Domain insertions in P2 and P4 preferential sites provide additional functions at the capsid outer surface, probably related to enzyme activity. The P2 insertion has a fold similar to that of gelsolin and profilin, two actin-binding proteins with a function in cytoskeleton metabolism, whereas the P4 insertion suggests protease activity involved in cleavage of the P2 383-residue C-terminal region, absent in the mature viral particle. Our results indicate that the intimate virus-fungus partnership has altered the capsid genome-protective and/or receptor-binding functions. Fungal virus evolution has tended to allocate enzyme activities to the virus capsid outer surface.</subfield>
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      <subfield code="a">PLoS Pathog. 2017 Dec 8;13(12):e1006755.</subfield>
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      <subfield code="a">10.1371/journal.ppat.1006755</subfield>
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      <subfield code="a">1553-7374</subfield>
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      <subfield code="a">1553-7374</subfield>
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      <subfield code="a">PLoS pathogens</subfield>
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      <subfield code="a">29220409</subfield>
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      <subfield code="a">http://hdl.handle.net/20.500.12105/6619</subfield>
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   <datafield ind2="0" ind1="0" tag="245">
      <subfield code="a">Acquisition of functions on the outer capsid surface during evolution of double-stranded RNA fungal viruses</subfield>
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