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Article: Hepatitis C virus glycoproteins interact with DC-SIGN and DC-SIGNR

TitleHepatitis C virus glycoproteins interact with DC-SIGN and DC-SIGNR
Authors
Issue Date2003
PublisherAmerican Society for Microbiology. The Journal's web site is located at http://jvi.asm.org/
Citation
Journal Of Virology, 2003, v. 77 n. 7, p. 4070-4080 How to Cite?
AbstractDC-SIGN and DC-SIGNR are two closely related membrane-associated C-type lectins that bind human immunodeficiency virus (HIV) envelope glycoprotein with high affinity. Binding of HIV to cells expressing DC-SIGN or DC-SIGNR can enhance the efficiency of infection of cells coexpressing the specific HIV receptors. DC-SIGN is expressed on some dendritic cells, while DC-SIGNR is localized to certain endothelial cell populations, including hepatic sinusoidal endothelial cells. We found that soluble versions of the hepatitis C virus (HCV) E2 glycoprotein and retrovirus pseudotypes expressing chimeric forms of both HCV E1 and E2 glycoproteins bound efficiently to DC-SIGN and DC-SIGNR expressed on cell lines and primary human endothelial cells but not to other C-type lectins tested. Soluble E2 bound to immature and mature human monocyte-derived dendritic cells (MDDCs). Binding of E2 to immature MDDCs was dependent on DC-SIGN interactions, while binding to mature MDDCs was partly independent of DC-SIGN, suggesting that other cell surface molecules may mediate HCV glycoprotein interactions. HCV interactions with DC-SIGN and DC-SIGNR may contribute to the establishment or persistence of infection both by the capture and delivery of virus to the liver and by modulating dendritic cell function.
Persistent Identifierhttp://hdl.handle.net/10722/157354
ISSN
2015 Impact Factor: 4.606
2015 SCImago Journal Rankings: 3.347
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorPöhlmann, Sen_US
dc.contributor.authorZhang, Jen_US
dc.contributor.authorBaribaud, Fen_US
dc.contributor.authorChen, Zen_US
dc.contributor.authorLeslie, GJen_US
dc.contributor.authorLin, Gen_US
dc.contributor.authorGranelliPiperno, Aen_US
dc.contributor.authorDoms, RWen_US
dc.contributor.authorRice, CMen_US
dc.contributor.authorMckeating, JAen_US
dc.date.accessioned2012-08-08T08:49:10Z-
dc.date.available2012-08-08T08:49:10Z-
dc.date.issued2003en_US
dc.identifier.citationJournal Of Virology, 2003, v. 77 n. 7, p. 4070-4080en_US
dc.identifier.issn0022-538Xen_US
dc.identifier.urihttp://hdl.handle.net/10722/157354-
dc.description.abstractDC-SIGN and DC-SIGNR are two closely related membrane-associated C-type lectins that bind human immunodeficiency virus (HIV) envelope glycoprotein with high affinity. Binding of HIV to cells expressing DC-SIGN or DC-SIGNR can enhance the efficiency of infection of cells coexpressing the specific HIV receptors. DC-SIGN is expressed on some dendritic cells, while DC-SIGNR is localized to certain endothelial cell populations, including hepatic sinusoidal endothelial cells. We found that soluble versions of the hepatitis C virus (HCV) E2 glycoprotein and retrovirus pseudotypes expressing chimeric forms of both HCV E1 and E2 glycoproteins bound efficiently to DC-SIGN and DC-SIGNR expressed on cell lines and primary human endothelial cells but not to other C-type lectins tested. Soluble E2 bound to immature and mature human monocyte-derived dendritic cells (MDDCs). Binding of E2 to immature MDDCs was dependent on DC-SIGN interactions, while binding to mature MDDCs was partly independent of DC-SIGN, suggesting that other cell surface molecules may mediate HCV glycoprotein interactions. HCV interactions with DC-SIGN and DC-SIGNR may contribute to the establishment or persistence of infection both by the capture and delivery of virus to the liver and by modulating dendritic cell function.en_US
dc.languageengen_US
dc.publisherAmerican Society for Microbiology. The Journal's web site is located at http://jvi.asm.org/en_US
dc.relation.ispartofJournal of Virologyen_US
dc.subject.meshAnimalsen_US
dc.subject.meshCell Adhesion Molecules - Metabolismen_US
dc.subject.meshCell Lineen_US
dc.subject.meshCells, Cultureden_US
dc.subject.meshDendritic Cells - Metabolism - Virologyen_US
dc.subject.meshEndothelium, Vascular - Metabolism - Virologyen_US
dc.subject.meshHiv - Genetics - Metabolismen_US
dc.subject.meshHepacivirus - Genetics - Metabolism - Pathogenicityen_US
dc.subject.meshHumansen_US
dc.subject.meshLectins - Metabolismen_US
dc.subject.meshLectins, C-Type - Metabolismen_US
dc.subject.meshProtein Bindingen_US
dc.subject.meshReceptors, Cell Surface - Metabolismen_US
dc.subject.meshSolubilityen_US
dc.subject.meshViral Envelope Proteins - Genetics - Metabolismen_US
dc.titleHepatitis C virus glycoproteins interact with DC-SIGN and DC-SIGNRen_US
dc.typeArticleen_US
dc.identifier.emailChen, Z:zchenai@hkucc.hku.hken_US
dc.identifier.authorityChen, Z=rp00243en_US
dc.description.naturelink_to_subscribed_fulltexten_US
dc.identifier.doi10.1128/JVI.77.7.4070-4080.2003en_US
dc.identifier.pmid12634366-
dc.identifier.scopuseid_2-s2.0-0037379186en_US
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-0037379186&selection=ref&src=s&origin=recordpageen_US
dc.identifier.volume77en_US
dc.identifier.issue7en_US
dc.identifier.spage4070en_US
dc.identifier.epage4080en_US
dc.identifier.isiWOS:000181677900018-
dc.publisher.placeUnited Statesen_US
dc.identifier.scopusauthoridPöhlmann, S=7003508167en_US
dc.identifier.scopusauthoridZhang, J=55168812200en_US
dc.identifier.scopusauthoridBaribaud, F=6602132353en_US
dc.identifier.scopusauthoridChen, Z=35271180800en_US
dc.identifier.scopusauthoridLeslie, GJ=7102173674en_US
dc.identifier.scopusauthoridLin, G=36780207400en_US
dc.identifier.scopusauthoridGranelliPiperno, A=7003981607en_US
dc.identifier.scopusauthoridDoms, RW=7007070550en_US
dc.identifier.scopusauthoridRice, CM=7201456901en_US
dc.identifier.scopusauthoridMcKeating, JA=35495802400en_US

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