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<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Redirecting Lentiviral Vectors Pseudotyped with Sindbis Virus-Derived Envelope Proteins to DC-SIGN by Modification of N-Linked Glycans of Envelope Proteins <xref ref-type="fn" rid="fn2">▿</xref>
</title>
<author><name sortKey="Morizono, Kouki" sort="Morizono, Kouki" uniqKey="Morizono K" first="Kouki" last="Morizono">Kouki Morizono</name>
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<author><name sortKey="Ku, Amy" sort="Ku, Amy" uniqKey="Ku A" first="Amy" last="Ku">Amy Ku</name>
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<author><name sortKey="Xie, Yiming" sort="Xie, Yiming" uniqKey="Xie Y" first="Yiming" last="Xie">Yiming Xie</name>
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<author><name sortKey="Harui, Airi" sort="Harui, Airi" uniqKey="Harui A" first="Airi" last="Harui">Airi Harui</name>
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<author><name sortKey="Kung, Sam K P" sort="Kung, Sam K P" uniqKey="Kung S" first="Sam K. P." last="Kung">Sam K. P. Kung</name>
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<author><name sortKey="Roth, Michael D" sort="Roth, Michael D" uniqKey="Roth M" first="Michael D." last="Roth">Michael D. Roth</name>
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</affiliation>
<affiliation><nlm:aff id="aff1"></nlm:aff>
</affiliation>
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<author><name sortKey="Lee, Benhur" sort="Lee, Benhur" uniqKey="Lee B" first="Benhur" last="Lee">Benhur Lee</name>
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</affiliation>
<affiliation><nlm:aff id="aff1"></nlm:aff>
</affiliation>
</author>
<author><name sortKey="Chen, Irvin S Y" sort="Chen, Irvin S Y" uniqKey="Chen I" first="Irvin S. Y." last="Chen">Irvin S. Y. Chen</name>
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</affiliation>
<affiliation><nlm:aff id="aff1"></nlm:aff>
</affiliation>
<affiliation><nlm:aff id="aff1"></nlm:aff>
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<publicationStmt><idno type="wicri:source">PMC</idno>
<idno type="pmid">20484510</idno>
<idno type="pmc">2898243</idno>
<idno type="url">http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2898243</idno>
<idno type="RBID">PMC:2898243</idno>
<idno type="doi">10.1128/JVI.00435-10</idno>
<date when="2010">2010</date>
<idno type="wicri:Area/Pmc/Corpus">000461</idno>
<idno type="wicri:explorRef" wicri:stream="Pmc" wicri:step="Corpus" wicri:corpus="PMC">000461</idno>
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<sourceDesc><biblStruct><analytic><title xml:lang="en" level="a" type="main">Redirecting Lentiviral Vectors Pseudotyped with Sindbis Virus-Derived Envelope Proteins to DC-SIGN by Modification of N-Linked Glycans of Envelope Proteins <xref ref-type="fn" rid="fn2">▿</xref>
</title>
<author><name sortKey="Morizono, Kouki" sort="Morizono, Kouki" uniqKey="Morizono K" first="Kouki" last="Morizono">Kouki Morizono</name>
<affiliation><nlm:aff id="aff1"></nlm:aff>
</affiliation>
<affiliation><nlm:aff id="aff1"></nlm:aff>
</affiliation>
</author>
<author><name sortKey="Ku, Amy" sort="Ku, Amy" uniqKey="Ku A" first="Amy" last="Ku">Amy Ku</name>
<affiliation><nlm:aff id="aff1"></nlm:aff>
</affiliation>
<affiliation><nlm:aff id="aff1"></nlm:aff>
</affiliation>
</author>
<author><name sortKey="Xie, Yiming" sort="Xie, Yiming" uniqKey="Xie Y" first="Yiming" last="Xie">Yiming Xie</name>
<affiliation><nlm:aff id="aff1"></nlm:aff>
</affiliation>
<affiliation><nlm:aff id="aff1"></nlm:aff>
</affiliation>
</author>
<author><name sortKey="Harui, Airi" sort="Harui, Airi" uniqKey="Harui A" first="Airi" last="Harui">Airi Harui</name>
<affiliation><nlm:aff id="aff1"></nlm:aff>
</affiliation>
</author>
<author><name sortKey="Kung, Sam K P" sort="Kung, Sam K P" uniqKey="Kung S" first="Sam K. P." last="Kung">Sam K. P. Kung</name>
<affiliation><nlm:aff id="aff1"></nlm:aff>
</affiliation>
<affiliation><nlm:aff id="aff1"></nlm:aff>
</affiliation>
</author>
<author><name sortKey="Roth, Michael D" sort="Roth, Michael D" uniqKey="Roth M" first="Michael D." last="Roth">Michael D. Roth</name>
<affiliation><nlm:aff id="aff1"></nlm:aff>
</affiliation>
<affiliation><nlm:aff id="aff1"></nlm:aff>
</affiliation>
</author>
<author><name sortKey="Lee, Benhur" sort="Lee, Benhur" uniqKey="Lee B" first="Benhur" last="Lee">Benhur Lee</name>
<affiliation><nlm:aff id="aff1"></nlm:aff>
</affiliation>
<affiliation><nlm:aff id="aff1"></nlm:aff>
</affiliation>
</author>
<author><name sortKey="Chen, Irvin S Y" sort="Chen, Irvin S Y" uniqKey="Chen I" first="Irvin S. Y." last="Chen">Irvin S. Y. Chen</name>
<affiliation><nlm:aff id="aff1"></nlm:aff>
</affiliation>
<affiliation><nlm:aff id="aff1"></nlm:aff>
</affiliation>
<affiliation><nlm:aff id="aff1"></nlm:aff>
</affiliation>
</author>
</analytic>
<series><title level="j">Journal of Virology</title>
<idno type="ISSN">0022-538X</idno>
<idno type="eISSN">1098-5514</idno>
<imprint><date when="2010">2010</date>
</imprint>
</series>
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<front><div type="abstract" xml:lang="en"><p>Redirecting the tropism of viral vectors enables specific transduction of selected cells by direct administration of vectors. We previously developed targeting lentiviral vectors by pseudotyping with modified Sindbis virus envelope proteins. These modified Sindbis virus envelope proteins have mutations in their original receptor-binding regions to eliminate their natural tropisms, and they are conjugated with targeting proteins, including antibodies and peptides, to confer their tropisms on target cells. We investigated whether our targeting vectors interact with DC-SIGN, which traps many types of viruses and gene therapy vectors by binding to the N-glycans of their envelope proteins. We found that these vectors do not interact with DC-SIGN. When these vectors were produced in the presence of deoxymannojirimycin, which alters the structures of N-glycans from complex to high mannose, these vectors used DC-SIGN as their receptor. Genetic analysis demonstrated that the N-glycans at E2 amino acid (aa) 196 and E1 aa 139 mediate binding to DC-SIGN, which supports the results of a previous report of cryoelectron microscopy analysis. In addition, we investigated whether modification of the N-glycan structures could activate serum complement activity, possibly by the lectin pathway of complement activation. DC-SIGN-targeted transduction occurs in the presence of human serum complement, demonstrating that high-mannose structure N-glycans of the envelope proteins do not activate human serum complement. These results indicate that the strategy of redirecting viral vectors according to alterations of their N-glycan structures would enable the vectors to target specific cells types expressing particular types of lectins.</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 Virol</journal-id>
<journal-id journal-id-type="publisher-id">jvirol</journal-id>
<journal-title-group><journal-title>Journal of Virology</journal-title>
</journal-title-group>
<issn pub-type="ppub">0022-538X</issn>
<issn pub-type="epub">1098-5514</issn>
<publisher><publisher-name>American Society for Microbiology (ASM)</publisher-name>
</publisher>
</journal-meta>
<article-meta><article-id pub-id-type="pmid">20484510</article-id>
<article-id pub-id-type="pmc">2898243</article-id>
<article-id pub-id-type="publisher-id">0435-10</article-id>
<article-id pub-id-type="doi">10.1128/JVI.00435-10</article-id>
<article-categories><subj-group subj-group-type="heading"><subject>Gene Delivery</subject>
</subj-group>
</article-categories>
<title-group><article-title>Redirecting Lentiviral Vectors Pseudotyped with Sindbis Virus-Derived Envelope Proteins to DC-SIGN by Modification of N-Linked Glycans of Envelope Proteins <xref ref-type="fn" rid="fn2">▿</xref>
</article-title>
</title-group>
<contrib-group><contrib contrib-type="author"><name><surname>Morizono</surname>
<given-names>Kouki</given-names>
</name>
<xref ref-type="aff" rid="aff1">1</xref>
<xref ref-type="aff" rid="aff1">2</xref>
</contrib>
<contrib contrib-type="author"><name><surname>Ku</surname>
<given-names>Amy</given-names>
</name>
<xref ref-type="aff" rid="aff1">1</xref>
<xref ref-type="aff" rid="aff1">2</xref>
</contrib>
<contrib contrib-type="author"><name><surname>Xie</surname>
<given-names>Yiming</given-names>
</name>
<xref ref-type="aff" rid="aff1">2</xref>
<xref ref-type="aff" rid="aff1">3</xref>
</contrib>
<contrib contrib-type="author"><name><surname>Harui</surname>
<given-names>Airi</given-names>
</name>
<xref ref-type="aff" rid="aff1">4</xref>
</contrib>
<contrib contrib-type="author"><name><surname>Kung</surname>
<given-names>Sam K. P.</given-names>
</name>
<xref ref-type="aff" rid="aff1">1</xref>
<xref ref-type="aff" rid="aff1">2</xref>
<xref ref-type="fn" rid="fn1">†</xref>
</contrib>
<contrib contrib-type="author"><name><surname>Roth</surname>
<given-names>Michael D.</given-names>
</name>
<xref ref-type="aff" rid="aff1">4</xref>
<xref ref-type="aff" rid="aff1">5</xref>
</contrib>
<contrib contrib-type="author"><name><surname>Lee</surname>
<given-names>Benhur</given-names>
</name>
<xref ref-type="aff" rid="aff1">2</xref>
<xref ref-type="aff" rid="aff1">3</xref>
</contrib>
<contrib contrib-type="author"><name><surname>Chen</surname>
<given-names>Irvin S. Y.</given-names>
</name>
<xref ref-type="aff" rid="aff1">1</xref>
<xref ref-type="aff" rid="aff1">2</xref>
<xref ref-type="aff" rid="aff1">3</xref>
<xref ref-type="corresp" rid="cor1">*</xref>
</contrib>
</contrib-group>
<aff id="aff1">Division of Hematology and Oncology, Department of Medicine, David Geffen School of Medicine, University of California, Los Angeles, California 90095,<label>1</label>
UCLA AIDS Institute, David Geffen School of Medicine, University of California, Los Angeles, California 90095,<label>2</label>
Departments of Microbiology, Immunology, and Molecular Genetics, David Geffen School of Medicine, University of California, Los Angeles, California 90095,<label>3</label>
Division of Pulmonary and Critical Care, Department of Medicine, David Geffen School of Medicine, University of California, Los Angeles, California 90095,<label>4</label>
Interdepartmental Program in Molecular Toxicology, David Geffen School of Medicine, University of California, Los Angeles, California 90095<label>5</label>
</aff>
<author-notes><corresp id="cor1"><label>*</label>
Corresponding author. Mailing address: Department of Medicine, David Geffen School of Medicine, University of California, Los Angeles, BSRB 173, Charles E. Young Dr. South, Los Angeles, CA 90095. Phone: (310) 825-4793. Fax: (310) 267-1875. E-mail: <email>syuchen@mednet.ucla.edu</email>
</corresp>
<fn id="fn1"><label>†</label>
<p>Present address: Laboratory of Innate Immunobiology, Department of Immunology, University of Manitoba, Winnipeg, Manitoba, Canada.</p>
</fn>
</author-notes>
<pub-date pub-type="ppub"><month>7</month>
<year>2010</year>
</pub-date>
<pub-date pub-type="epub"><day>19</day>
<month>5</month>
<year>2010</year>
</pub-date>
<volume>84</volume>
<issue>14</issue>
<fpage>6923</fpage>
<lpage>6934</lpage>
<history><date date-type="received"><day>26</day>
<month>2</month>
<year>2010</year>
</date>
<date date-type="accepted"><day>6</day>
<month>5</month>
<year>2010</year>
</date>
</history>
<permissions><copyright-statement>Copyright © 2010, American Society for Microbiology</copyright-statement>
<copyright-year>2010</copyright-year>
</permissions>
<self-uri xlink:title="pdf" xlink:href="zjv01410006923.pdf"></self-uri>
<abstract><p>Redirecting the tropism of viral vectors enables specific transduction of selected cells by direct administration of vectors. We previously developed targeting lentiviral vectors by pseudotyping with modified Sindbis virus envelope proteins. These modified Sindbis virus envelope proteins have mutations in their original receptor-binding regions to eliminate their natural tropisms, and they are conjugated with targeting proteins, including antibodies and peptides, to confer their tropisms on target cells. We investigated whether our targeting vectors interact with DC-SIGN, which traps many types of viruses and gene therapy vectors by binding to the N-glycans of their envelope proteins. We found that these vectors do not interact with DC-SIGN. When these vectors were produced in the presence of deoxymannojirimycin, which alters the structures of N-glycans from complex to high mannose, these vectors used DC-SIGN as their receptor. Genetic analysis demonstrated that the N-glycans at E2 amino acid (aa) 196 and E1 aa 139 mediate binding to DC-SIGN, which supports the results of a previous report of cryoelectron microscopy analysis. In addition, we investigated whether modification of the N-glycan structures could activate serum complement activity, possibly by the lectin pathway of complement activation. DC-SIGN-targeted transduction occurs in the presence of human serum complement, demonstrating that high-mannose structure N-glycans of the envelope proteins do not activate human serum complement. These results indicate that the strategy of redirecting viral vectors according to alterations of their N-glycan structures would enable the vectors to target specific cells types expressing particular types of lectins.</p>
</abstract>
</article-meta>
</front>
</pmc>
</record>
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