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            <name>Title</name>
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                <text>Coronavirus</text>
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                <text>Dominio científico: Coronavirus</text>
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              <text>Human monoclonal antibodies against highly conserved HR1 and HR2 domains of the SARS-CoV spike protein are more broadly neutralizing.</text>
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          <name>Creator</name>
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              <text>Hatem A Elshabrawy, Melissa M. Coughlin, Susan C. Baker, Bellur S. Prabhakar</text>
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              <text>Immune sera from convalescent patients have been shown to be effective in the treatment of patients infected with Severe Acute Respiratory Syndrome Virus (SARS-CoV) making passive immune therapy with human monoclonal antibodies an attractive treatment strategy for SARS. Previously, using Xenomouse (Amgen British Columbia Inc), we produced a panel of neutralizing Human monoclonal antibodies (HmAbs) that could specifically bind to the ectodomain of the SARS-CoV spike (S) glycoprotein. Some of the HmAbs were S1 domain specific, while some were not. In this study, we describe non-S1 binding neutralizing HmAbs that can specifically bind to the conserved S2 domain of the S protein. However, unlike the S1 specific HmAbs, the S2 specific HmAbs can neutralize pseudotyped viruses expressing different S proteins containing receptor binding domain sequences of various clinical isolates. These data indicate that HmAbs which bind to conserved regions of the S protein are more suitable for conferring protection against a wide range of SARS-CoV variants and have implications for generating therapeutic antibodies or subunit vaccines against other enveloped viruses.</text>
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              <text>2012</text>
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              <text>DOI: 10.1371/journal.pone.0050366</text>
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              <text>PLoS ONE</text>
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              <text>Public Library of Science (PLoS)</text>
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              <text>Science, Medicine</text>
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              <text>EN</text>
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