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Characterization of a Heparan Sulfate Octasaccharide that Binds to Herpes Simplex Viral Type 1 Glycoprotein D

dc.rights.licenseOpen Access
dc.rights.licenseA full text version is available in DSpace@RPI
dc.contributor.authorLiu, J.
dc.contributor.authorShriver, Z.
dc.contributor.authorPope, R.M.
dc.contributor.authorThorp, S.C.
dc.contributor.authorRaska, C.S.
dc.contributor.authorYoshida, K.
dc.contributor.authorEisenberg, R.J.
dc.contributor.authorCohen, G.
dc.contributor.authorLinhardt, Robert J.
dc.contributor.authorSasisekharan, R.
dc.date2002
dc.date.accessioned2022-06-23T01:39:17Z
dc.date.available2022-06-23T01:39:17Z
dc.date.issued2002
dc.identifier.citationCharacterization of a Heparan Sulfate Octasaccharide that Binds to Herpes Simplex Viral Type 1 Glycoprotein D, J. Liu, Z. Shriver, R.M. Pope, S.C. Thorp, C.S. Raska, K. Yoshida, R.J. Eisenberg, G. Cohen, R.J. Linhardt, R. Sasisekharan, Journal of Biological Chemistry, 277,33456-33467. 2002.
dc.identifier.urihttps://doi.org/10.1074/jbc.M202034200
dc.descriptionJournal of Biological Chemistry, 277,33456-33467
dc.descriptionNote : if this item contains full text it may be a preprint, author manuscript, or a Gold OA copy that permits redistribution with a license such as CC BY. The final version is available through the publisher’s platform.
dc.description.abstractHerpes simplex virus type 1 utilizes cell surface heparan sulfate as receptors to infect target cells. The unique heparan sulfate saccharide sequence offers the binding site for viral envelope proteins and plays critical roles in assisting viral infections. A specific 3-O-sulfated heparan sulfate is known to facilitate the entry of herpes simplex virus 1 into cells. The 3-O-sulfated heparan sulfate is generated by the heparan sulfate d-glucosaminyl-3-O-sulfotransferase isoform 3 (3-OST-3), and it provides binding sites for viral glycoprotein D (gD). Here, we report the purification and structural characterization of an oligosaccharide that binds to gD. The isolated gD-binding site is an octasaccharide, and has a binding affinity to gD around 18 microm, as determined by affinity coelectrophoresis. The octasaccharide was prepared and purified from a heparan sulfate oligosaccharide library that was modified by purified 3-OST-3 enzyme. The molecular mass of the isolated octasaccharide was determined using both nanoelectrospray ionization mass spectrometry and matrix-assisted laser desorption/ionization mass spectrometry. The results from the sequence analysis suggest that the structure of the octasaccharide is a heptasulfated octasaccharide. The proposed structure of the octasaccharide is DeltaUA-GlcNS-IdoUA2S-GlcNAc-UA2S-GlcNS-IdoUA2S-GlcNH(2)3S6S. Given that the binding of 3-O-sulfated heparan sulfate to gD can mediate viral entry, our results provide structural information about heparan sulfate-assisted viral entry.
dc.languageENG
dc.language.isoen_US
dc.publisherElsevier
dc.relation.ispartofThe Linhardt Research Labs Online Collection
dc.relation.ispartofRensselaer Polytechnic Institute, Troy, NY
dc.relation.urihttps://harc.rpi.edu/
dc.rightsAttribution 3.0 United States*
dc.rights.urihttp://creativecommons.org/licenses/by/3.0/us/*
dc.subjectBiology
dc.subjectChemistry and chemical biology
dc.subjectChemical and biological engineering
dc.subjectBiomedical engineering
dc.titleCharacterization of a Heparan Sulfate Octasaccharide that Binds to Herpes Simplex Viral Type 1 Glycoprotein Den_US
dc.titleCharacterization of a Heparan Sulfate Octasaccharide that Binds to Herpes Simplex Viral Type 1 Glycoprotein D
dc.typeArticle
dcterms.accessRightsA full text version is available in DSpace@RPI
dcterms.isVersionOfhttps://doi.org/10.1074/jbc.M202034200
dc.rights.holderCC BY : this license allows reusers to distribute, remix, adapt, and build upon the material in any medium or format, so long as attribution is given to the creator. The license allows for commercial use. Credit must be given to the authors and the original work must be properly cited.
dc.creator.identifierhttps://orcid.org/0000-0003-2219-5833
dc.relation.departmentThe Linhardt Research Labs.
dc.relation.departmentThe Shirley Ann Jackson, Ph.D. Center for Biotechnology and Interdisciplinary Studies (CBIS)


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