Journal article
Characterization of a heparan sulfate octasaccharide that binds to herpes simplex virus type 1 glycoprotein D
The Journal of biological chemistry, Vol.277(36), pp.33456-33467
09/06/2002
DOI: 10.1074/jbc.M202034200
PMID: 12080045
Abstract
Herpes 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.
Details
- Title: Subtitle
- Characterization of a heparan sulfate octasaccharide that binds to herpes simplex virus type 1 glycoprotein D
- Creators
- Jian Liu - University of North Carolina at Chapel HillZach Shriver - Massachusetts Institute of TechnologyR Marshall Pope - University of North Carolina at Chapel HillSuzanne C Thorp - University of North Carolina at Chapel HillMichael B Duncan - University of North Carolina at Chapel HillRonald J Copeland - University of North Carolina at Chapel HillChristina S Raska - University of North Carolina at Chapel HillKeiichi YoshidaRoselyn J Eisenberg - University of PennsylvaniaGary Cohen - University of PennsylvaniaRobert J Linhardt - University of IowaRam Sasisekharan - Massachusetts Institute of Technology
- Resource Type
- Journal article
- Publication Details
- The Journal of biological chemistry, Vol.277(36), pp.33456-33467
- DOI
- 10.1074/jbc.M202034200
- PMID
- 12080045
- ISSN
- 0021-9258
- eISSN
- 1083-351X
- Grant note
- CA 090940 / NCI NIH HHS R01 HL 59479 / NHLBI NIH HHS AI50050-01 / NIAID NIH HHS P01 HL 41484 / NHLBI NIH HHS GM 57073 / NIGMS NIH HHS
- Language
- English
- Date published
- 09/06/2002
- Academic Unit
- Medicine Administration
- Record Identifier
- 9984632134002771
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