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            <name>Title</name>
            <description>A name given to the resource</description>
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                <text>Coronavirus</text>
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            <description>An account of the resource</description>
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                <text>Dominio científico: Coronavirus</text>
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          <name>Title</name>
          <description>A name given to the resource</description>
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              <text>In Situ Tagged nsp15 Reveals Interactions with Coronavirus Replication/Transcription Complex-Associated Proteins</text>
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          <name>Creator</name>
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              <text>Jeremiah Athmer, Anthony R. Fehr, Matthew Grunewald, Everett Clinton Smith, Mark R. Denison, Stanley Perlman, Peter Palese</text>
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          <name>Description</name>
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              <text>Coronavirus (CoV) replication and transcription are carried out in close proximity to restructured endoplasmic reticulum (ER) membranes in replication/transcription complexes (RTC). Many of the CoV nonstructural proteins (nsps) are required for RTC function; however, not all of their functions are known. nsp15 contains an endoribonuclease domain that is conserved in the CoV family. While the enzymatic activity and crystal structure of nsp15 are well defined, its role in replication remains elusive. nsp15 localizes to sites of RNA replication, but whether it acts independently or requires additional interactions for its function remains unknown. To begin to address these questions, we created an in situ tagged form of nsp15 using the prototypic CoV, mouse hepatitis virus (MHV). In MHV, nsp15 contains the genomic RNA packaging signal (P/S), a 95-bp RNA stem-loop structure that is not required for viral replication or nsp15 function. Utilizing this knowledge, we constructed an internal hemagglutinin (HA) tag that replaced the P/S. We found that nsp15-HA was localized to discrete perinuclear puncta and strongly colocalized with nsp8 and nsp12, both well-defined members of the RTC, but not the membrane (M) protein, involved in virus assembly. Finally, we found that nsp15 interacted with RTC-associated proteins nsp8 and nsp12 during infection, and this interaction was RNA independent. From this, we conclude that nsp15 localizes and interacts with CoV proteins in the RTC, suggesting it plays a direct or indirect role in virus replication. Furthermore, the use of in situ epitope tags could be used to determine novel nsp-nsp interactions in coronaviruses.</text>
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              <text>2017</text>
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          <name>Identifier</name>
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              <text>DOI: 10.1128/mBio.02320-16</text>
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          <name>Source</name>
          <description>A related resource from which the described resource is derived</description>
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              <text>mBio</text>
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          <name>Publisher</name>
          <description>An entity responsible for making the resource available</description>
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              <text>American Society for Microbiology</text>
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          <name>Coverage</name>
          <description>The spatial or temporal topic of the resource, the spatial applicability of the resource, or the jurisdiction under which the resource is relevant</description>
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              <text>Microbiology</text>
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          <name>Language</name>
          <description>A language of the resource</description>
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              <text>EN</text>
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