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<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Potent Human Monoclonal Antibodies against SARS CoV, Nipah and Hendra Viruses</title><author><name sortKey="Prabakaran, Ponraj" sort="Prabakaran, Ponraj" uniqKey="Prabakaran P" first="Ponraj" last="Prabakaran">Ponraj Prabakaran</name><affiliation><nlm:aff id="A1">Protein Interactions Group, CCRNP, CCR, NCI-Frederick, NIH, Frederick, MD 21702</nlm:aff></affiliation></author><author><name sortKey="Zhongyu, Zhu" sort="Zhongyu, Zhu" uniqKey="Zhongyu Z" first="Zhu" last="Zhongyu">Zhu Zhongyu</name><affiliation><nlm:aff id="A1">Protein Interactions Group, CCRNP, CCR, NCI-Frederick, NIH, Frederick, MD 21702</nlm:aff></affiliation><affiliation><nlm:aff id="A2">BRP, SAIC-Frederick, Inc., NCI-Frederick, Frederick, MD 21702</nlm:aff></affiliation></author><author><name sortKey="Xiao, Xiaodong" sort="Xiao, Xiaodong" uniqKey="Xiao X" first="Xiaodong" last="Xiao">Xiaodong Xiao</name><affiliation><nlm:aff id="A1">Protein Interactions Group, CCRNP, CCR, NCI-Frederick, NIH, Frederick, MD 21702</nlm:aff></affiliation></author><author><name sortKey="Biragyn, Arya" sort="Biragyn, Arya" uniqKey="Biragyn A" first="Arya" last="Biragyn">Arya Biragyn</name><affiliation><nlm:aff id="A3">Laboratory of Immunology, Gerontology Research Center, National Institute on Aging, Baltimore, MD 21224</nlm:aff></affiliation></author><author><name sortKey="Dimitrov, Antony S" sort="Dimitrov, Antony S" uniqKey="Dimitrov A" first="Antony S." last="Dimitrov">Antony S. Dimitrov</name><affiliation><nlm:aff id="A4">Department of Microbiology and Immunology, Uniformed Services University, Bethesda, MD 20814</nlm:aff></affiliation></author><author><name sortKey="Broder, Christopher C" sort="Broder, Christopher C" uniqKey="Broder C" first="Christopher C." last="Broder">Christopher C. Broder</name><affiliation><nlm:aff id="A4">Department of Microbiology and Immunology, Uniformed Services University, Bethesda, MD 20814</nlm:aff></affiliation></author><author><name sortKey="Dimitrov, Dimiter S" sort="Dimitrov, Dimiter S" uniqKey="Dimitrov D" first="Dimiter S." last="Dimitrov">Dimiter S. Dimitrov</name><affiliation><nlm:aff id="A1">Protein Interactions Group, CCRNP, CCR, NCI-Frederick, NIH, Frederick, MD 21702</nlm:aff></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">PMC</idno><idno type="pmid">19216624</idno><idno type="pmc">2705284</idno><idno type="url">http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2705284</idno><idno type="RBID">PMC:2705284</idno><idno type="doi">10.1517/14712590902763755</idno><date when="2009">2009</date><idno type="wicri:Area/Pmc/Corpus">000C11</idno><idno type="wicri:explorRef" wicri:stream="Pmc" wicri:step="Corpus" wicri:corpus="PMC">000C11</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en" level="a" type="main">Potent Human Monoclonal Antibodies against SARS CoV, Nipah and Hendra Viruses</title><author><name sortKey="Prabakaran, Ponraj" sort="Prabakaran, Ponraj" uniqKey="Prabakaran P" first="Ponraj" last="Prabakaran">Ponraj Prabakaran</name><affiliation><nlm:aff id="A1">Protein Interactions Group, CCRNP, CCR, NCI-Frederick, NIH, Frederick, MD 21702</nlm:aff></affiliation></author><author><name sortKey="Zhongyu, Zhu" sort="Zhongyu, Zhu" uniqKey="Zhongyu Z" first="Zhu" last="Zhongyu">Zhu Zhongyu</name><affiliation><nlm:aff id="A1">Protein Interactions Group, CCRNP, CCR, NCI-Frederick, NIH, Frederick, MD 21702</nlm:aff></affiliation><affiliation><nlm:aff id="A2">BRP, SAIC-Frederick, Inc., NCI-Frederick, Frederick, MD 21702</nlm:aff></affiliation></author><author><name sortKey="Xiao, Xiaodong" sort="Xiao, Xiaodong" uniqKey="Xiao X" first="Xiaodong" last="Xiao">Xiaodong Xiao</name><affiliation><nlm:aff id="A1">Protein Interactions Group, CCRNP, CCR, NCI-Frederick, NIH, Frederick, MD 21702</nlm:aff></affiliation></author><author><name sortKey="Biragyn, Arya" sort="Biragyn, Arya" uniqKey="Biragyn A" first="Arya" last="Biragyn">Arya Biragyn</name><affiliation><nlm:aff id="A3">Laboratory of Immunology, Gerontology Research Center, National Institute on Aging, Baltimore, MD 21224</nlm:aff></affiliation></author><author><name sortKey="Dimitrov, Antony S" sort="Dimitrov, Antony S" uniqKey="Dimitrov A" first="Antony S." last="Dimitrov">Antony S. Dimitrov</name><affiliation><nlm:aff id="A4">Department of Microbiology and Immunology, Uniformed Services University, Bethesda, MD 20814</nlm:aff></affiliation></author><author><name sortKey="Broder, Christopher C" sort="Broder, Christopher C" uniqKey="Broder C" first="Christopher C." last="Broder">Christopher C. Broder</name><affiliation><nlm:aff id="A4">Department of Microbiology and Immunology, Uniformed Services University, Bethesda, MD 20814</nlm:aff></affiliation></author><author><name sortKey="Dimitrov, Dimiter S" sort="Dimitrov, Dimiter S" uniqKey="Dimitrov D" first="Dimiter S." last="Dimitrov">Dimiter S. Dimitrov</name><affiliation><nlm:aff id="A1">Protein Interactions Group, CCRNP, CCR, NCI-Frederick, NIH, Frederick, MD 21702</nlm:aff></affiliation></author></analytic><series><title level="j">Expert opinion on biological therapy</title><idno type="ISSN">1471-2598</idno><idno type="eISSN">1744-7682</idno><imprint><date when="2009">2009</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en"><p id="P4">Polyclonal antibodies have a century-old history of being effective against some viruses; recently, monoclonal antibodies (mAbs) have also shown success. The humanized mAb Synagis (palivizumab) remains still the only mAb against respiratory syncytial virus (RSV) infections approved by the U.S. Food and Drug Administration (FDA). Recently, several potent human monoclonal antibodies (hmAbs) targeting the Severe Acute Respiratory Syndrome-Associated coronavirus (SARS CoV) S glycoproteins were developed quickly after the virus was identified in 2003. Among these antibodies, m396 and S230.15 exhibit exceptional potency and cross-reactivity as they neutralize isolates from the first and second outbreaks and from palm civets both <italic>in vitro</italic>and in mice. Similarly, the first fully hmAbs against two other paramyxoviruses, Hendra virus (HeV) and Nipah virus (NiV), which can cause up to 75% mortality, were recently developed; one of them, m102.4, shows exceptional cross-reactive potency against both NiV and HeV. Three-dimensional molecular structures of envelope glycoproteins from these viruses in complexes with antibodies and/or receptors were recently determined. Structural analyses along with other experiments have provided insights into the molecular mechanisms of receptor recognition and antibody neutralization, and suggested that these antibodies alone or in combination could successfully fight the viruses’ heterogeneity and mutability which is a major problem in the development of effective therapeutic agents against viruses, including therapeutic antibodies.</p></div></front></TEI><pmc article-type="research-article" xml:lang="EN"><pmc-comment>The publisher of this article does not allow downloading of the full text in XML form.</pmc-comment>
<pmc-dir>properties manuscript</pmc-dir>
<front><journal-meta><journal-id journal-id-type="nlm-journal-id">101125414</journal-id><journal-id journal-id-type="pubmed-jr-id">26807</journal-id><journal-id journal-id-type="nlm-ta">Expert Opin Biol Ther</journal-id><journal-title>Expert opinion on biological therapy</journal-title><issn pub-type="ppub">1471-2598</issn><issn pub-type="epub">1744-7682</issn></journal-meta><article-meta><article-id pub-id-type="pmid">19216624</article-id><article-id pub-id-type="pmc">2705284</article-id><article-id pub-id-type="doi">10.1517/14712590902763755</article-id><article-id pub-id-type="manuscript">NIHMS93623</article-id><article-categories><subj-group subj-group-type="heading"><subject>Article</subject></subj-group></article-categories><title-group><article-title>Potent Human Monoclonal Antibodies against SARS CoV, Nipah and Hendra Viruses</article-title></title-group><contrib-group><contrib contrib-type="author"><name><surname>Prabakaran</surname><given-names>Ponraj</given-names></name><xref ref-type="author-notes" rid="FN3">§</xref><xref ref-type="aff" rid="A1">1</xref><xref ref-type="author-notes" rid="FN1">2</xref><xref ref-type="corresp" rid="cor1">*</xref></contrib><contrib contrib-type="author"><name><surname>Zhongyu</surname><given-names>Zhu</given-names></name><xref ref-type="author-notes" rid="FN3">§</xref><xref ref-type="aff" rid="A1">1</xref><xref ref-type="aff" rid="A2">3</xref></contrib><contrib contrib-type="author"><name><surname>Xiao</surname><given-names>Xiaodong</given-names></name><xref ref-type="aff" rid="A1">1</xref></contrib><contrib contrib-type="author"><name><surname>Biragyn</surname><given-names>Arya</given-names></name><xref ref-type="aff" rid="A3">4</xref></contrib><contrib contrib-type="author"><name><surname>Dimitrov</surname><given-names>Antony S.</given-names></name><xref ref-type="author-notes" rid="FN2">5</xref><xref ref-type="aff" rid="A4">6</xref></contrib><contrib contrib-type="author"><name><surname>Broder</surname><given-names>Christopher C.</given-names></name><xref ref-type="aff" rid="A4">6</xref></contrib><contrib contrib-type="author"><name><surname>Dimitrov</surname><given-names>Dimiter S.</given-names></name><xref ref-type="aff" rid="A1">1</xref><xref ref-type="corresp" rid="cor1">*</xref></contrib></contrib-group><aff id="A1"><label>1</label>Protein Interactions Group, CCRNP, CCR, NCI-Frederick, NIH, Frederick, MD 21702</aff><aff id="A2"><label>3</label>BRP, SAIC-Frederick, Inc., NCI-Frederick, Frederick, MD 21702</aff><aff id="A3"><label>4</label>Laboratory of Immunology, Gerontology Research Center, National Institute on Aging, Baltimore, MD 21224</aff><aff id="A4"><label>6</label>Department of Microbiology and Immunology, Uniformed Services University, Bethesda, MD 20814</aff><author-notes><fn id="FN1" fn-type="present-address"><label>2</label><p id="P1">Current address: Duke Human Vaccine Institute, Duke University Medical Center, Durham, NC 27710</p></fn><fn id="FN2" fn-type="present-address"><label>5</label><p id="P2">Current address: Profectus BioSciences, Inc., Techcenter at UMBC, 1450 South Rolling Road, Baltimore, MD 21227</p></fn><fn id="FN3" fn-type="equal"><label>§</label><p id="P3">Authors contributed equally</p></fn><corresp id="cor1"><label>*</label>Authors for correspondence, Prabakaran Ponraj, Duke Human Vaccine Institute, 106 Research Drive, MSRBII, 3013, Box 103020 DUMC, Duke University Medical Center, Durham, NC 27710, Phone: 919-668-2680, Fax: 919-684-5230, E-mail: <email>prabakaran.ponraj@duke.edu</email>, Dimiter S. Dimitrov, Protein Interactions, CCRNP, NCI-Frederick, NIH, Bldg 469, 150B, P.O. Box B, Miller Drive, Frederick, MD 21702-1201, Phone: 301-846-1352, Fax: 301-846-5598, E-mail: <email>dimitrov@ncifcrf.gov</email></corresp></author-notes><pub-date pub-type="nihms-submitted"><day>20</day><month>2</month><year>2009</year></pub-date><pub-date pub-type="ppub"><month>3</month><year>2009</year></pub-date><pub-date pub-type="pmc-release"><day>1</day><month>3</month><year>2010</year></pub-date><volume>9</volume><issue>3</issue><fpage>355</fpage><lpage>368</lpage><abstract><p id="P4">Polyclonal antibodies have a century-old history of being effective against some viruses; recently, monoclonal antibodies (mAbs) have also shown success. The humanized mAb Synagis (palivizumab) remains still the only mAb against respiratory syncytial virus (RSV) infections approved by the U.S. Food and Drug Administration (FDA). Recently, several potent human monoclonal antibodies (hmAbs) targeting the Severe Acute Respiratory Syndrome-Associated coronavirus (SARS CoV) S glycoproteins were developed quickly after the virus was identified in 2003. Among these antibodies, m396 and S230.15 exhibit exceptional potency and cross-reactivity as they neutralize isolates from the first and second outbreaks and from palm civets both <italic>in vitro</italic>and in mice. Similarly, the first fully hmAbs against two other paramyxoviruses, Hendra virus (HeV) and Nipah virus (NiV), which can cause up to 75% mortality, were recently developed; one of them, m102.4, shows exceptional cross-reactive potency against both NiV and HeV. Three-dimensional molecular structures of envelope glycoproteins from these viruses in complexes with antibodies and/or receptors were recently determined. Structural analyses along with other experiments have provided insights into the molecular mechanisms of receptor recognition and antibody neutralization, and suggested that these antibodies alone or in combination could successfully fight the viruses’ heterogeneity and mutability which is a major problem in the development of effective therapeutic agents against viruses, including therapeutic antibodies.</p></abstract><kwd-group><kwd>antibody</kwd><kwd>SARS CoV</kwd><kwd>Hendra virus</kwd><kwd>Nipah virus</kwd><kwd>therapeutics</kwd><kwd>vaccines</kwd></kwd-group><contract-num rid="AI1">U54 AI057168-05S20013</contract-num><contract-num rid="AI1">U54 AI057168-010002</contract-num><contract-sponsor id="AI1">National Institute of Allergy and Infectious Diseases Extramural Activities : NIAID</contract-sponsor></article-meta></front></pmc></record>Pour manipuler ce document sous Unix (Dilib)
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