On a mouse monoclonal antibody that neutralizes all four dengue virus serotypes
Identifieur interne : 001966 ( Pmc/Corpus ); précédent : 001965; suivant : 001967On a mouse monoclonal antibody that neutralizes all four dengue virus serotypes
Auteurs : Ravikumar Rajamanonmani ; Celine Nkenfou ; Paula Clancy ; Yin Hoe Yau ; Susana Geifman Shochat ; Soila Sukupolvi-Petty ; Wouter Schul ; Michael S. Diamond ; Subhash G. Vasudevan ; Julien LescarSource :
- The Journal of General Virology [ 0022-1317 ] ; 2009.
Abstract
The flavivirus envelope glycoprotein (E) is responsible for viral attachment and entry by membrane fusion. Its ectodomain is the primary target of the humoral immune response. In particular, the C-terminal Ig-like domain III of E, which is exposed at the surface of the viral particle, forms an attractive antigen for raising protective monoclonal antibodies (mAb). 9F12, a mouse mAb raised against a dengue virus (DENV) serotype 2 recombinant domain III, cross-reacts with corresponding domains from the other three DENV serotypes and also with West Nile virus. mAb 9F12 binds with nanomolar affinity to a conserved epitope that maps to the viral surface comprising residues 305, 307, 310 and 330 of the E protein. mAb 9F12 neutralizes all four DENV serotypes in plaque reduction assays. We expressed a single-chain Fv from 9F12 that retains the binding activity of the parent mAb. Adsorption and fusion inhibition assays indicate that mAb 9F12 prevents early steps of viral entry. Its virus inhibition activity and broad cross-reactivity makes mAb 9F12 a suitable candidate for optimization and humanization into a therapeutic antibody to treat severe infections by dengue.
Url:
DOI: 10.1099/vir.0.006874-0
PubMed: 19264660
PubMed Central: 2889437
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PMC:2889437Le document en format XML
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<author><name sortKey="Rajamanonmani, Ravikumar" sort="Rajamanonmani, Ravikumar" uniqKey="Rajamanonmani R" first="Ravikumar" last="Rajamanonmani">Ravikumar Rajamanonmani</name>
<affiliation><nlm:aff id="aff1">School of Biological Sciences, Nanyang Technological University, Biopolis, Singapore</nlm:aff>
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<affiliation><nlm:aff id="aff5">Program in Emerging Infectious Diseases, Duke-NUS, Graduate Medical School, Singapore</nlm:aff>
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<author><name sortKey="Clancy, Paula" sort="Clancy, Paula" uniqKey="Clancy P" first="Paula" last="Clancy">Paula Clancy</name>
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<author><name sortKey="Vasudevan, Subhash G" sort="Vasudevan, Subhash G" uniqKey="Vasudevan S" first="Subhash G." last="Vasudevan">Subhash G. Vasudevan</name>
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<idno type="ISSN">0022-1317</idno>
<idno type="eISSN">1465-2099</idno>
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<front><div type="abstract" xml:lang="en"><p>The flavivirus envelope glycoprotein (E) is responsible for viral attachment and entry by membrane fusion. Its ectodomain is the primary target of the humoral immune response. In particular, the C-terminal Ig-like domain III of E, which is exposed at the surface of the viral particle, forms an attractive antigen for raising protective monoclonal antibodies (mAb). 9F12, a mouse mAb raised against a dengue virus (DENV) serotype 2 recombinant domain III, cross-reacts with corresponding domains from the other three DENV serotypes and also with West Nile virus. mAb 9F12 binds with nanomolar affinity to a conserved epitope that maps to the viral surface comprising residues 305, 307, 310 and 330 of the E protein. mAb 9F12 neutralizes all four DENV serotypes in plaque reduction assays. We expressed a single-chain Fv from 9F12 that retains the binding activity of the parent mAb. Adsorption and fusion inhibition assays indicate that mAb 9F12 prevents early steps of viral entry. Its virus inhibition activity and broad cross-reactivity makes mAb 9F12 a suitable candidate for optimization and humanization into a therapeutic antibody to treat severe infections by dengue.</p>
</div>
</front>
</TEI>
<pmc article-type="research-article"><pmc-comment>The publisher of this article does not allow downloading of the full text in XML form.</pmc-comment>
<front><journal-meta><journal-id journal-id-type="nlm-ta">J Gen Virol</journal-id>
<journal-id journal-id-type="publisher-id">vir</journal-id>
<journal-title-group><journal-title>The Journal of General Virology</journal-title>
</journal-title-group>
<issn pub-type="ppub">0022-1317</issn>
<issn pub-type="epub">1465-2099</issn>
<publisher><publisher-name>Society for General Microbiology</publisher-name>
</publisher>
</journal-meta>
<article-meta><article-id pub-id-type="pmid">19264660</article-id>
<article-id pub-id-type="pmc">2889437</article-id>
<article-id pub-id-type="publisher-id">799</article-id>
<article-id pub-id-type="doi">10.1099/vir.0.006874-0</article-id>
<article-categories><subj-group subj-group-type="heading"><subject>Animal</subject>
</subj-group>
</article-categories>
<title-group><article-title>On a mouse monoclonal antibody that neutralizes all four dengue virus serotypes</article-title>
</title-group>
<contrib-group><contrib contrib-type="author"><name><surname>Rajamanonmani</surname>
<given-names>Ravikumar</given-names>
</name>
<xref ref-type="aff" rid="aff1">1</xref>
<xref ref-type="aff" rid="aff5">5</xref>
</contrib>
<contrib contrib-type="author"><name><surname>Nkenfou</surname>
<given-names>Celine</given-names>
</name>
<xref ref-type="aff" rid="aff2">2</xref>
</contrib>
<contrib contrib-type="author"><name><surname>Clancy</surname>
<given-names>Paula</given-names>
</name>
<xref ref-type="aff" rid="aff3">3</xref>
</contrib>
<contrib contrib-type="author"><name><surname>Yau</surname>
<given-names>Yin Hoe</given-names>
</name>
<xref ref-type="aff" rid="aff1">1</xref>
</contrib>
<contrib contrib-type="author"><name><surname>Shochat</surname>
<given-names>Susana Geifman</given-names>
</name>
<xref ref-type="aff" rid="aff1">1</xref>
</contrib>
<contrib contrib-type="author"><name><surname>Sukupolvi-Petty</surname>
<given-names>Soila</given-names>
</name>
<xref ref-type="aff" rid="aff4">4</xref>
</contrib>
<contrib contrib-type="author"><name><surname>Schul</surname>
<given-names>Wouter</given-names>
</name>
<xref ref-type="aff" rid="aff2">2</xref>
</contrib>
<contrib contrib-type="author"><name><surname>Diamond</surname>
<given-names>Michael S.</given-names>
</name>
<xref ref-type="aff" rid="aff4">4</xref>
</contrib>
<contrib contrib-type="author"><name><surname>Vasudevan</surname>
<given-names>Subhash G.</given-names>
</name>
<xref ref-type="aff" rid="aff3">3</xref>
<xref ref-type="aff" rid="aff5">5</xref>
</contrib>
<contrib contrib-type="author"><name><surname>Lescar</surname>
<given-names>Julien</given-names>
</name>
<xref ref-type="aff" rid="aff1">1</xref>
<xref ref-type="aff" rid="aff6">6</xref>
</contrib>
</contrib-group>
<aff id="aff1"><label>1</label>
School of Biological Sciences, Nanyang Technological University, Biopolis, Singapore</aff>
<aff id="aff2"><label>2</label>
Novartis Institute for Tropical Diseases, Biopolis, Singapore</aff>
<aff id="aff3"><label>3</label>
Department of Biochemistry and Molecular Biology, James Cook University, Australia</aff>
<aff id="aff4"><label>4</label>
Departments of Medicine, Molecular Microbiology, Pathology and Immunology, Washington University School of Medicine, St Louis, USA</aff>
<aff id="aff5"><label>5</label>
Program in Emerging Infectious Diseases, Duke-NUS, Graduate Medical School, Singapore</aff>
<aff id="aff6"><label>6</label>
AFMB CNRS UMR6098, Marseille, France</aff>
<author-notes><corresp><bold>Correspondence</bold>
: Julien Lescar: <email>julien@ntu.edu.sg</email>
: Subhash G. Vasudevan: <email>subhash.vasudevan@duke-nus.edu.sg</email>
</corresp>
</author-notes>
<pub-date pub-type="ppub"><month>4</month>
<year>2009</year>
</pub-date>
<pub-date pub-type="pmc-release"><day>1</day>
<month>4</month>
<year>2010</year>
</pub-date>
<pmc-comment> PMC Release delay is 12 months and 0 days and was based on the copyright element. </pmc-comment>
<volume>90</volume>
<issue>Pt 4</issue>
<fpage>799</fpage>
<lpage>809</lpage>
<history><date date-type="received"><day>28</day>
<month>8</month>
<year>2008</year>
</date>
<date date-type="accepted"><day>7</day>
<month>12</month>
<year>2008</year>
</date>
</history>
<permissions><copyright-statement>Copyright © 2009, SGM</copyright-statement>
<copyright-year>2009</copyright-year>
</permissions>
<self-uri xlink:title="pdf" xlink:href="799.pdf"></self-uri>
<abstract><p>The flavivirus envelope glycoprotein (E) is responsible for viral attachment and entry by membrane fusion. Its ectodomain is the primary target of the humoral immune response. In particular, the C-terminal Ig-like domain III of E, which is exposed at the surface of the viral particle, forms an attractive antigen for raising protective monoclonal antibodies (mAb). 9F12, a mouse mAb raised against a dengue virus (DENV) serotype 2 recombinant domain III, cross-reacts with corresponding domains from the other three DENV serotypes and also with West Nile virus. mAb 9F12 binds with nanomolar affinity to a conserved epitope that maps to the viral surface comprising residues 305, 307, 310 and 330 of the E protein. mAb 9F12 neutralizes all four DENV serotypes in plaque reduction assays. We expressed a single-chain Fv from 9F12 that retains the binding activity of the parent mAb. Adsorption and fusion inhibition assays indicate that mAb 9F12 prevents early steps of viral entry. Its virus inhibition activity and broad cross-reactivity makes mAb 9F12 a suitable candidate for optimization and humanization into a therapeutic antibody to treat severe infections by dengue.</p>
</abstract>
</article-meta>
</front>
</pmc>
</record>
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