Herpes Simplex Virus Glycoprotein D Bound to the Human Receptor HveA

Carfı́, Andrea; Willis, Sharon H.; Whitbeck, J. Charles; Krummenacher, Claude; Cohen, Gary H.; Eisenberg, Roselyn J.; Wiley, Don C.

doi:10.1016/s1097-2765(01)00298-2

Cited by 347 publications

(495 citation statements)

References 63 publications

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“…It is believed that the interaction between gD and the 3-O-sulfated HS triggers the fusion between the virus and the cell in the presence of other viral envelope proteins, including gB, gH, and gL, via an uncharacterized mechanism. The study of the crystal structure of gD and herpes entry receptor HveA suggest that the binding of HveA to gD induces conformational changes in gD (21). This study also predicts a 3-O-sulfated HS-binding pocket on gD near the HveA-binding site (21).…”

Section: -O-sulfotransferase Isoform 3 (3-ost-3) and It Provides Bimentioning

confidence: 62%

“…The study of the crystal structure of gD and herpes entry receptor HveA suggest that the binding of HveA to gD induces conformational changes in gD (21). This study also predicts a 3-O-sulfated HS-binding pocket on gD near the HveA-binding site (21). The exact carbohydrate sequence of the gD-binding site in 3-Osulfated HS remains to be investigated.…”

Section: -O-sulfotransferase Isoform 3 (3-ost-3) and It Provides Bimentioning

confidence: 72%

“…Two possibilities may contribute to the lower binding affinity. First, two domains in gD for binding to 3-O-sulfated HS were predicted by Carfi and colleagues (21). It is possible that the HS polysaccharide interacts with both sites, whereas the octasaccharide is insufficiently large to bind at both sites.…”

Section: Discussionmentioning

confidence: 99%

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Characterization of a Heparan Sulfate Octasaccharide That Binds to Herpes Simplex Virus Type 1 Glycoprotein D

Liu

Shriver

Pope

et al. 2002

Journal of Biological Chemistry

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153

116

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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 gDbinding site is an octasaccharide, and has a binding affinity to gD around 18 M, 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 ⌬UA-GlcNSIdoUA2S-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.Heparan sulfates (HS), 1 highly sulfated polysaccharides, are present on the surface of mammalian cells and in the extracellular matrix in large quantities. HS play critical roles in a variety of biological interactions, including assisting viral infection, regulating blood coagulation and embryonic development, suppressing tumor growth, and controlling the eating behavior of mice by interacting with specific regulatory proteins (1-5). HS is initially synthesized as a copolymer of glucuronic acid and N-acetylated glucosamine by D-glucuronyl and N-acetyl-D-glucosaminyl transferase, followed by various modifications (6). These modifications include C 5 -epimerization of glucuronic acid to form iduronic acid residues, 2-O-sulfation of iduronic and glucuronic acid, N-deacetylation and N-sulfation of glucosamine, as well as 6-O-sulfation and 3-O-sulfation of glucosamine. Numerous HS biosynthetic enzymes have been cloned and characterized (for review, see Esko and Lindahl (7)).The specific sulfated saccharide sequences play critical roles in determining the functions of HS. A recent report suggests that the expression levels of various isoforms of each class of HS biosynthetic enzyme contribute to the synthesis of specific saccharide sequences in specific tissues (8). HS N-deacetylase/ N-sulfotransferase, 3-O-sulfotransferase, and 6-O-sulfotransferase are present in multiple isoforms, and each isoform is believed to recognize the saccharide sequence around the modification site to generate a specific sulfated saccharid...

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Section: -O-sulfotransferase Isoform 3 (3-ost-3) and It Provides Bimentioning

confidence: 62%

Section: -O-sulfotransferase Isoform 3 (3-ost-3) and It Provides Bimentioning

confidence: 72%

See 1 more Smart Citation

Characterization of a Heparan Sulfate Octasaccharide That Binds to Herpes Simplex Virus Type 1 Glycoprotein D

Liu

Shriver

Pope

et al. 2002

Journal of Biological Chemistry

Self Cite

153

116

View full text Add to dashboard Cite

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“…These results are in agreement with crystal structure data pinpointing the binding site for HveA and demonstrate that HveA binding to the N-terminus of gD results in a conformational change that may be responsible for inducing virus envelope fusion with the cell surface. 59,60 Together, these studies suggest that HveA is recognized by a folded part of gD that can be affected by mutations spanning a substantial portion of the molecule.…”

Section: Virus Attachment and Entrymentioning

confidence: 87%

“…54 In addition, domains within gD have been defined that specifically interact with either HveA or HveC (Shah et al, unpublished data). 57,60,[67][68][69]125,126 This understanding of the basic biology of HSV-1 binding and entry has enabled the development of HSV vectors designed to target specifically distinct cell populations.…”

Section: Retargeting Hsv-1 To Specific Cell Typesmentioning

confidence: 99%

HSV trafficking and development of gene therapy vectors with applications in the nervous system

et al. 2005

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Herpes simplex virus type 1 (HSV-1) is a neurotropic doublestranded DNA virus that causes cold sores, keratitis, and rarely encephalitis in humans. Nonpathogenic HSV-1 gene transfer vectors have been generated by elimination of viral functions necessary for replication. The life cycle of the native virus includes replication in epithelial cells at the site of initial inoculation followed by retrograde axonal transport to the nuclei of sensory neurons innervating the area of cutaneous primary infection. In this review, we summarize the current understanding of the molecular basis for HSV cell entry, nuclear transport of the genome, virion egress following replication, and retrograde and anterograde axonal transport in neurons. We discuss how each of these properties has been exploited or modified to allow the generation of gene transfer vectors with particular utility for neurological applications. Recent advances in engineering virus entry have provided proof of principle that vector targeting is possible. Furthermore, significant and potentially therapeutic modifications to the pathological responses to various noxious insults have been demonstrated in models of peripheral nerve disease. These applications exploit the natural axonal transport mechanism of HSV, allowing transgene expression in the cell nucleus within the inaccessible trigeminal ganglion or dorsal root ganglion, following the noninvasive procedure of subcutaneous vector inoculation. These findings demonstrate the importance of understanding basic virology in the design of vector systems and the powerful approach of exploiting favorable properties of the parent virus in the generation of gene transfer vectors. Gene Therapy (2005) 12, 891-901.

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Nanotechnologies for Targeted Delivery of Drugs

Brož

Hunziker

2003

Nanotechnologies for the Life Sciences

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The sections in this article are Introduction Basic and Special Pharmacology Outline Basic Pharmacology Absorption Bioavailability Distribution Elimination Special Pharmacology Skin Epithelium Mucosal Epithelium of the Respiratory Tract Mucosal Epithelium of the Gastrointestinal Tract Mononuclear Phagocyte System ( MPS ) Endothelial Barrier Cell Membrane Strategies for Targeted Delivery – Observed in Nature Outline Bacteria Host Invasion Immune System Evasion Viruses Immune System Evasion Host Cell Invasion Viral Vectors for Therapeutic Applications Prions Strategies for Targeted Delivery – Designed by Man Outline Noninvasive Delivery Systems Oral Delivery Systems Transdermal Delivery Systems Transmucosal Delivery Systems Invasive Delivery Systems Targeted Delivery to the Brain Macrophage Targeting Other Targets Conclusion and Outlook

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Herpes Simplex Virus Glycoprotein D Bound to the Human Receptor HveA

Cited by 347 publications

References 63 publications

Characterization of a Heparan Sulfate Octasaccharide That Binds to Herpes Simplex Virus Type 1 Glycoprotein D

Characterization of a Heparan Sulfate Octasaccharide That Binds to Herpes Simplex Virus Type 1 Glycoprotein D

HSV trafficking and development of gene therapy vectors with applications in the nervous system

Nanotechnologies for Targeted Delivery of Drugs

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