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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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            <name>Description</name>
            <description>An account of the resource</description>
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                <text>Dominio científico: Coronavirus</text>
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    <name>Text</name>
    <description>A resource consisting primarily of words for reading. Examples include books, letters, dissertations, poems, newspapers, articles, archives of mailing lists. Note that facsimiles or images of texts are still of the genre Text.</description>
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      <name>Dublin Core</name>
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          <name>Title</name>
          <description>A name given to the resource</description>
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              <text>Neutralizing antibodies against porcine epidemic diarrhea virus block virus attachment and internalization</text>
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          <name>Creator</name>
          <description>An entity primarily responsible for making the resource</description>
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              <text>Lang Gong, Ying Lin, Jianru Qin, Qianniu Li, Chunyi Xue, Yongchang Cao</text>
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        <element elementId="41">
          <name>Description</name>
          <description>An account of the resource</description>
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              <text>Abstract Background Porcine epidemic diarrhea virus (PEDV) is emerging as a pathogenic coronavirus that causes a huge economic burden to the swine industry. Interaction of the viral spike (S) surface glycoprotein with the host cell receptor is recognized as the first step of infection and is the main determinant of virus tropism. The mechanisms by which neutralizing antibodies inhibit PEDV have not been defined. Isolating PEDV neutralizing antibodies are crucial to identifying the receptor-binding domains of the viral spike and elucidating the mechanism of protection against PEDV infection. Methods B cell hybridoma technique was used to generate hybridoma cells that secrete specific antibodies. E.coli prokaryotic expression system and Bac-to-Bac expression system were used to identify the target protein of each monoclonal antibody. qPCR was performed to analyze PEDV binding to Vero E6 cells with neutralizing antibody. Results We identified 10 monoclonal antibodies using hybridoma technology. Remarkably, 4 mAbs (designed 2G8, 2B11, 3D9, 1E3) neutralized virus infection potently, of which 2B11 and 1E3 targeted the conformational epitope of the PEDV S protein. qPCR results showed that both 2B11 and 2G8 blocked virus entry into Vero cells. Conclusion The data suggested that PEDV neutralizing antibody inhibited virus infection by binding to infectious virions, which could work as a tool to find the receptor-binding domains.</text>
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          <name>Date</name>
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              <text>2018</text>
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          <name>Subject</name>
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              <text>porcine epidemic diarrhea virus, S protein, neutralizing antibody, Attachment</text>
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          <name>Identifier</name>
          <description>An unambiguous reference to the resource within a given context</description>
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              <text>DOI: 10.1186/s12985-018-1042-3</text>
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          <name>Source</name>
          <description>A related resource from which the described resource is derived</description>
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            <elementText elementTextId="21458">
              <text>Virology Journal</text>
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          <name>Publisher</name>
          <description>An entity responsible for making the resource available</description>
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              <text>BMC</text>
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          </elementTextContainer>
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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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            <elementText elementTextId="21460">
              <text>Infectious and parasitic diseases</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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