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<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Monomerization of the viral entry inhibitor griffithsin yields insights into the relationship between multivalent binding to high mannose oligosaccharides and antiviral activity</title><author><name sortKey="Moulaei, Tinoush" sort="Moulaei, Tinoush" uniqKey="Moulaei T" first="Tinoush" last="Moulaei">Tinoush Moulaei</name><affiliation><nlm:aff id="A1">Protein Structure Section, Macromolecular Crystallography Laboratory, National Cancer, Institute-Frederick, Frederick, MD 21702-1201, USA</nlm:aff></affiliation></author><author><name sortKey="Shenoy, Shilpa R" sort="Shenoy, Shilpa R" uniqKey="Shenoy S" first="Shilpa R." last="Shenoy">Shilpa R. Shenoy</name><affiliation><nlm:aff id="A2">Molecular Targets Laboratory, Center for Cancer Research, National Cancer Institute-Frederick, Frederick, MD 21702-1201, USA</nlm:aff></affiliation><affiliation><nlm:aff id="A3">SAIC-Frederick Inc., National Cancer Institute, Frederick, MD 21702-1201, USA</nlm:aff></affiliation></author><author><name sortKey="Giomarelli, Barbara" sort="Giomarelli, Barbara" uniqKey="Giomarelli B" first="Barbara" last="Giomarelli">Barbara Giomarelli</name><affiliation><nlm:aff id="A2">Molecular Targets Laboratory, Center for Cancer Research, National Cancer Institute-Frederick, Frederick, MD 21702-1201, USA</nlm:aff></affiliation></author><author><name sortKey="Thomas, Cheryl" sort="Thomas, Cheryl" uniqKey="Thomas C" first="Cheryl" last="Thomas">Cheryl Thomas</name><affiliation><nlm:aff id="A2">Molecular Targets Laboratory, Center for Cancer Research, National Cancer Institute-Frederick, Frederick, MD 21702-1201, USA</nlm:aff></affiliation></author><author><name sortKey="Mcmahon, James B" sort="Mcmahon, James B" uniqKey="Mcmahon J" first="James B." last="Mcmahon">James B. Mcmahon</name><affiliation><nlm:aff id="A2">Molecular Targets Laboratory, Center for Cancer Research, National Cancer Institute-Frederick, Frederick, MD 21702-1201, USA</nlm:aff></affiliation></author><author><name sortKey="Dauter, Zbigniew" sort="Dauter, Zbigniew" uniqKey="Dauter Z" first="Zbigniew" last="Dauter">Zbigniew Dauter</name><affiliation><nlm:aff id="A4">Synchrotron Radiation Research Section, Macromolecular Crystallography Laboratory, National Cancer Institute, Argonne National Laboratory, Argonne, IL 60439, USA</nlm:aff></affiliation></author><author><name sortKey="O Eefe, Barry R" sort="O Eefe, Barry R" uniqKey="O Eefe B" first="Barry R." last="O Eefe">Barry R. O Eefe</name><affiliation><nlm:aff id="A2">Molecular Targets Laboratory, Center for Cancer Research, National Cancer Institute-Frederick, Frederick, MD 21702-1201, USA</nlm:aff></affiliation></author><author><name sortKey="Wlodawer, Alexander" sort="Wlodawer, Alexander" uniqKey="Wlodawer A" first="Alexander" last="Wlodawer">Alexander Wlodawer</name><affiliation><nlm:aff id="A1">Protein Structure Section, Macromolecular Crystallography Laboratory, National Cancer, Institute-Frederick, Frederick, MD 21702-1201, USA</nlm:aff></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">PMC</idno><idno type="pmid">20826337</idno><idno type="pmc">3399781</idno><idno type="url">http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3399781</idno><idno type="RBID">PMC:3399781</idno><idno type="doi">10.1016/j.str.2010.05.016</idno><date when="2010">2010</date><idno type="wicri:Area/Pmc/Corpus">000757</idno><idno type="wicri:explorRef" wicri:stream="Pmc" wicri:step="Corpus" wicri:corpus="PMC">000757</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en" level="a" type="main">Monomerization of the viral entry inhibitor griffithsin yields insights into the relationship between multivalent binding to high mannose oligosaccharides and antiviral activity</title><author><name sortKey="Moulaei, Tinoush" sort="Moulaei, Tinoush" uniqKey="Moulaei T" first="Tinoush" last="Moulaei">Tinoush Moulaei</name><affiliation><nlm:aff id="A1">Protein Structure Section, Macromolecular Crystallography Laboratory, National Cancer, Institute-Frederick, Frederick, MD 21702-1201, USA</nlm:aff></affiliation></author><author><name sortKey="Shenoy, Shilpa R" sort="Shenoy, Shilpa R" uniqKey="Shenoy S" first="Shilpa R." last="Shenoy">Shilpa R. Shenoy</name><affiliation><nlm:aff id="A2">Molecular Targets Laboratory, Center for Cancer Research, National Cancer Institute-Frederick, Frederick, MD 21702-1201, USA</nlm:aff></affiliation><affiliation><nlm:aff id="A3">SAIC-Frederick Inc., National Cancer Institute, Frederick, MD 21702-1201, USA</nlm:aff></affiliation></author><author><name sortKey="Giomarelli, Barbara" sort="Giomarelli, Barbara" uniqKey="Giomarelli B" first="Barbara" last="Giomarelli">Barbara Giomarelli</name><affiliation><nlm:aff id="A2">Molecular Targets Laboratory, Center for Cancer Research, National Cancer Institute-Frederick, Frederick, MD 21702-1201, USA</nlm:aff></affiliation></author><author><name sortKey="Thomas, Cheryl" sort="Thomas, Cheryl" uniqKey="Thomas C" first="Cheryl" last="Thomas">Cheryl Thomas</name><affiliation><nlm:aff id="A2">Molecular Targets Laboratory, Center for Cancer Research, National Cancer Institute-Frederick, Frederick, MD 21702-1201, USA</nlm:aff></affiliation></author><author><name sortKey="Mcmahon, James B" sort="Mcmahon, James B" uniqKey="Mcmahon J" first="James B." last="Mcmahon">James B. Mcmahon</name><affiliation><nlm:aff id="A2">Molecular Targets Laboratory, Center for Cancer Research, National Cancer Institute-Frederick, Frederick, MD 21702-1201, USA</nlm:aff></affiliation></author><author><name sortKey="Dauter, Zbigniew" sort="Dauter, Zbigniew" uniqKey="Dauter Z" first="Zbigniew" last="Dauter">Zbigniew Dauter</name><affiliation><nlm:aff id="A4">Synchrotron Radiation Research Section, Macromolecular Crystallography Laboratory, National Cancer Institute, Argonne National Laboratory, Argonne, IL 60439, USA</nlm:aff></affiliation></author><author><name sortKey="O Eefe, Barry R" sort="O Eefe, Barry R" uniqKey="O Eefe B" first="Barry R." last="O Eefe">Barry R. O Eefe</name><affiliation><nlm:aff id="A2">Molecular Targets Laboratory, Center for Cancer Research, National Cancer Institute-Frederick, Frederick, MD 21702-1201, USA</nlm:aff></affiliation></author><author><name sortKey="Wlodawer, Alexander" sort="Wlodawer, Alexander" uniqKey="Wlodawer A" first="Alexander" last="Wlodawer">Alexander Wlodawer</name><affiliation><nlm:aff id="A1">Protein Structure Section, Macromolecular Crystallography Laboratory, National Cancer, Institute-Frederick, Frederick, MD 21702-1201, USA</nlm:aff></affiliation></author></analytic><series><title level="j">Structure(London, England:1993)</title><idno type="ISSN">0969-2126</idno><idno type="eISSN">1878-4186</idno><imprint><date when="2010">2010</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en"><title>SUMMARY</title><p id="P1">Mutations were introduced to the domain-swapped homodimer of the antiviral lectin griffithsin (GRFT). Whereas several single and double mutants remained dimeric, insertion of either two or four amino acids at the dimerization interface resulted in a monomeric form of the protein (mGRFT). Monomeric character of the modified proteins was confirmed by sedimentation equilibrium ultracentrifugation and by their high resolution X-ray crystal structures, whereas their binding to carbohydrates was assessed by isothermal titration calorimetry. Cell-based antiviral activity assays utilizing different variants of mGRFT indicated that the monomeric form of the lectin had greatly reduced activity against HIV-1, suggesting that the antiviral activity of GRFT stems from crosslinking and aggregation of viral particles via multivalent interactions between GRFT and oligosaccharides present on HIV envelope glycoproteins. Atomic resolution crystal structure of a complex between mGRFT and nonamannoside revealed that a single mGRFT molecule binds to two different nonamannoside molecules through all three carbohydrate-binding sites present on the monomer.</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>
<pmc-dir>properties manuscript</pmc-dir>
<front><journal-meta><journal-id journal-id-type="nlm-journal-id">101087697</journal-id><journal-id journal-id-type="pubmed-jr-id">22305</journal-id><journal-id journal-id-type="nlm-ta">Structure</journal-id><journal-id journal-id-type="iso-abbrev">Structure</journal-id><journal-title-group><journal-title>Structure(London, England:1993)</journal-title></journal-title-group><issn pub-type="ppub">0969-2126</issn><issn pub-type="epub">1878-4186</issn></journal-meta><article-meta><article-id pub-id-type="pmid">20826337</article-id><article-id pub-id-type="pmc">3399781</article-id><article-id pub-id-type="doi">10.1016/j.str.2010.05.016</article-id><article-id pub-id-type="manuscript">NIHMS388794</article-id><article-categories><subj-group subj-group-type="heading"><subject>Article</subject></subj-group></article-categories><title-group><article-title>Monomerization of the viral entry inhibitor griffithsin yields insights into the relationship between multivalent binding to high mannose oligosaccharides and antiviral activity</article-title></title-group><contrib-group><contrib contrib-type="author"><name><surname>Moulaei</surname><given-names>Tinoush</given-names></name><xref ref-type="aff" rid="A1">1</xref></contrib><contrib contrib-type="author"><name><surname>Shenoy</surname><given-names>Shilpa R.</given-names></name><xref ref-type="aff" rid="A2">2</xref><xref ref-type="aff" rid="A3">3</xref></contrib><contrib contrib-type="author"><name><surname>Giomarelli</surname><given-names>Barbara</given-names></name><xref ref-type="aff" rid="A2">2</xref></contrib><contrib contrib-type="author"><name><surname>Thomas</surname><given-names>Cheryl</given-names></name><xref ref-type="aff" rid="A2">2</xref></contrib><contrib contrib-type="author"><name><surname>McMahon</surname><given-names>James B.</given-names></name><xref ref-type="aff" rid="A2">2</xref></contrib><contrib contrib-type="author"><name><surname>Dauter</surname><given-names>Zbigniew</given-names></name><xref ref-type="aff" rid="A4">4</xref></contrib><contrib contrib-type="author"><name><surname>O’Keefe</surname><given-names>Barry R.</given-names></name><xref ref-type="aff" rid="A2">2</xref></contrib><contrib contrib-type="author"><name><surname>Wlodawer</surname><given-names>Alexander</given-names></name><xref ref-type="aff" rid="A1">1</xref></contrib></contrib-group><aff id="A1"><label>1</label>Protein Structure Section, Macromolecular Crystallography Laboratory, National Cancer, Institute-Frederick, Frederick, MD 21702-1201, USA</aff><aff id="A2"><label>2</label>Molecular Targets Laboratory, Center for Cancer Research, National Cancer Institute-Frederick, Frederick, MD 21702-1201, USA</aff><aff id="A3"><label>3</label>SAIC-Frederick Inc., National Cancer Institute, Frederick, MD 21702-1201, USA</aff><aff id="A4"><label>4</label>Synchrotron Radiation Research Section, Macromolecular Crystallography Laboratory, National Cancer Institute, Argonne National Laboratory, Argonne, IL 60439, USA</aff><author-notes><corresp id="CR1">Corresponding Author: Alexander Wlodawer, Macromolecular Crystallography Laboratory, NCI, Frederick, MD 21702-1201, Phone: +1-301-846-5036, Fax: +1-301-846-6322,<email>wlodawer@nih.gov</email>; Barry R. O’Keefe, Molecular Targets Laboratory, NCI, Frederick, MD 21702-1202, Phone: +1-301-846-5332, Fax: +1-301-846-6872, <email>okeefeba@mail.nih.gov</email></corresp></author-notes><pub-date pub-type="nihms-submitted"><day>26</day><month>6</month><year>2012</year></pub-date><pub-date pub-type="ppub"><day>8</day><month>9</month><year>2010</year></pub-date><pub-date pub-type="pmc-release"><day>18</day><month>7</month><year>2012</year></pub-date><volume>18</volume><issue>9</issue><fpage>1104</fpage><lpage>1115</lpage><abstract><title>SUMMARY</title><p id="P1">Mutations were introduced to the domain-swapped homodimer of the antiviral lectin griffithsin (GRFT). Whereas several single and double mutants remained dimeric, insertion of either two or four amino acids at the dimerization interface resulted in a monomeric form of the protein (mGRFT). Monomeric character of the modified proteins was confirmed by sedimentation equilibrium ultracentrifugation and by their high resolution X-ray crystal structures, whereas their binding to carbohydrates was assessed by isothermal titration calorimetry. Cell-based antiviral activity assays utilizing different variants of mGRFT indicated that the monomeric form of the lectin had greatly reduced activity against HIV-1, suggesting that the antiviral activity of GRFT stems from crosslinking and aggregation of viral particles via multivalent interactions between GRFT and oligosaccharides present on HIV envelope glycoproteins. Atomic resolution crystal structure of a complex between mGRFT and nonamannoside revealed that a single mGRFT molecule binds to two different nonamannoside molecules through all three carbohydrate-binding sites present on the monomer.</p></abstract><kwd-group><kwd>Lectin</kwd><kwd>Entry Inhibitor</kwd><kwd>HIV</kwd><kwd>Man9</kwd><kwd>High Mannose Oligosaccharide</kwd><kwd>Branched Carbohydrates</kwd><kwd>Griffithsin</kwd></kwd-group><funding-group><award-group><funding-source country="United States">Division of Basic Sciences : NCI</funding-source><award-id>ZIA BC010348-10 || BC</award-id></award-group></funding-group></article-meta></front></pmc></record>Pour manipuler ce document sous Unix (Dilib)
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