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Article: Addition of a single gp120 glycan confers increased binding to dendritic cell-specific ICAM-3-grabbing nonintegrin and neutralization escape to human immunodeficiency virus type 1

TitleAddition of a single gp120 glycan confers increased binding to dendritic cell-specific ICAM-3-grabbing nonintegrin and neutralization escape to human immunodeficiency virus type 1
Authors
Issue Date2002
PublisherAmerican Society for Microbiology. The Journal's web site is located at http://jvi.asm.org/
Citation
Journal Of Virology, 2002, v. 76 n. 20, p. 10299-10306 How to Cite?
AbstractThe potential role of dendritic cell-specific ICAM-3-grabbing nonintegrin (DC-SIGN) binding in human immunodeficiency virus transmission across the mucosal barrier was investigated by assessing the ability of simian-human immunodeficiency chimeric viruses (SHIVs) showing varying degrees of mucosal transmissibility to bind the DC-SIGN expressed on the surface of transfected cells. We found that gp120 of the highly transmissible, pathogenic CCR5-tropic SHIV SF162P3 bound human and rhesus DC-SIGN with an efficiency threefold or greater than that of gp120 of the nonpathogenic, poorly transmissible parental SHIV SF162, and this increase in binding to the DC-SIGN of the SHIV SF162P3 envelope gp120 translated into an enhancement of T-cell infection in trans. The presence of an additional glycan at the N-terminal base of the V2 loop of SHIV SF162P3 gp120 compared to that of the parental virus was shown to be responsible for the increase in binding to DC-SIGN. Interestingly, this glycan also conferred escape from autologous neutralization, raising the possibility that the modification occurred as a result of immune selection. Our data suggest that more-efficient binding of envelope gp120 to DC-SIGN could be relevant to the enhanced mucosal transmissibility of SHIV SF162P3 compared to that of parental SHIV SF162.
Persistent Identifierhttp://hdl.handle.net/10722/157343
ISSN
2015 Impact Factor: 4.606
2015 SCImago Journal Rankings: 3.347
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorLue, Jen_US
dc.contributor.authorHsu, Men_US
dc.contributor.authorYang, Den_US
dc.contributor.authorMarx, Pen_US
dc.contributor.authorChen, Zen_US
dc.contributor.authorChengMayer, Cen_US
dc.date.accessioned2012-08-08T08:49:04Z-
dc.date.available2012-08-08T08:49:04Z-
dc.date.issued2002en_US
dc.identifier.citationJournal Of Virology, 2002, v. 76 n. 20, p. 10299-10306en_US
dc.identifier.issn0022-538Xen_US
dc.identifier.urihttp://hdl.handle.net/10722/157343-
dc.description.abstractThe potential role of dendritic cell-specific ICAM-3-grabbing nonintegrin (DC-SIGN) binding in human immunodeficiency virus transmission across the mucosal barrier was investigated by assessing the ability of simian-human immunodeficiency chimeric viruses (SHIVs) showing varying degrees of mucosal transmissibility to bind the DC-SIGN expressed on the surface of transfected cells. We found that gp120 of the highly transmissible, pathogenic CCR5-tropic SHIV SF162P3 bound human and rhesus DC-SIGN with an efficiency threefold or greater than that of gp120 of the nonpathogenic, poorly transmissible parental SHIV SF162, and this increase in binding to the DC-SIGN of the SHIV SF162P3 envelope gp120 translated into an enhancement of T-cell infection in trans. The presence of an additional glycan at the N-terminal base of the V2 loop of SHIV SF162P3 gp120 compared to that of the parental virus was shown to be responsible for the increase in binding to DC-SIGN. Interestingly, this glycan also conferred escape from autologous neutralization, raising the possibility that the modification occurred as a result of immune selection. Our data suggest that more-efficient binding of envelope gp120 to DC-SIGN could be relevant to the enhanced mucosal transmissibility of SHIV SF162P3 compared to that of parental SHIV SF162.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.meshAntigens, Cd - Immunologyen_US
dc.subject.meshAntigens, Differentiation - Immunologyen_US
dc.subject.meshCell Adhesion Moleculesen_US
dc.subject.meshCell Line, Transformeden_US
dc.subject.meshDendritic Cells - Immunologyen_US
dc.subject.meshGlycosylationen_US
dc.subject.meshHiv Envelope Protein Gp120 - Immunologyen_US
dc.subject.meshHiv-1 - Immunologyen_US
dc.subject.meshHumansen_US
dc.subject.meshIntegrinsen_US
dc.subject.meshNeutralization Testsen_US
dc.subject.meshPolysaccharides - Immunologyen_US
dc.subject.meshSimian Immunodeficiency Virus - Immunologyen_US
dc.titleAddition of a single gp120 glycan confers increased binding to dendritic cell-specific ICAM-3-grabbing nonintegrin and neutralization escape to human immunodeficiency virus type 1en_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.76.20.10299-10306.2002en_US
dc.identifier.pmid12239306-
dc.identifier.scopuseid_2-s2.0-0036785596en_US
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-0036785596&selection=ref&src=s&origin=recordpageen_US
dc.identifier.volume76en_US
dc.identifier.issue20en_US
dc.identifier.spage10299en_US
dc.identifier.epage10306en_US
dc.identifier.isiWOS:000178319600024-
dc.publisher.placeUnited Statesen_US
dc.identifier.scopusauthoridLue, J=15025041900en_US
dc.identifier.scopusauthoridHsu, M=7202371039en_US
dc.identifier.scopusauthoridYang, D=7404801484en_US
dc.identifier.scopusauthoridMarx, P=7102894750en_US
dc.identifier.scopusauthoridChen, Z=35271180800en_US
dc.identifier.scopusauthoridChengMayer, C=7005778878en_US

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