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Chondroitin sulfate...
Chondroitin sulfate characterized by the E-disaccharide unit is a potent inhibitor of herpes simplex virus infectivity and provides the virus binding sites on gro2C cells.
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- Bergefall, Kicki, 1975 (author)
- Gothenburg University,Göteborgs universitet,Institutionen för laboratoriemedicin, Avdelningen för klinisk virologi,Institute of Laboratory Medicine, Dept of Clinical Virology
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- Trybala, Edward, 1955 (author)
- Gothenburg University,Göteborgs universitet,Institutionen för laboratoriemedicin, Avdelningen för klinisk virologi,Institute of Laboratory Medicine, Dept of Clinical Virology
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- Johansson, Maria, 1971 (author)
- Gothenburg University,Göteborgs universitet,Institutionen för laboratoriemedicin, Avdelningen för klinisk virologi,Institute of Laboratory Medicine, Dept of Clinical Virology
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Uyama, Toru (author)
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Naito, Satomi (author)
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Yamada, Shuhei (author)
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Kitagawa, Hiroshi (author)
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Sugahara, Kazuyuki (author)
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- Bergström, Tomas, 1950 (author)
- Gothenburg University,Göteborgs universitet,Institutionen för laboratoriemedicin, Avdelningen för klinisk virologi,Institute of Laboratory Medicine, Dept of Clinical Virology
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(creator_code:org_t)
- 2005
- 2005
- English.
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In: The Journal of biological chemistry. - 0021-9258. ; 280:37, s. 32193-9
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https://doi.org/10.1...
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Abstract
Subject headings
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- Although cell surface chondroitin sulfate (CS) is regarded as an auxiliary receptor for binding of herpes simplex virus to cells, and purified CS chain types A, B, and C are known to interfere poorly or not at all with the virus infection of cells, we have found that CS type E (CS-E), derived from squid cartilage, exhibited potent antiviral activity. The IC(50) values ranged from 0.06 to 0.2 mug/ml and substantially exceeded the antiviral potency of heparin, the known inhibitor of virus binding to cells. Furthermore, in mutant gro2C cells that express CS but not heparan sulfate, CS-E showed unusually high anti-herpes virus activity with IC(50) values of <1 ng/ml. Enzymatic degradation of CS-E with chondroitinase ABC abolished its antiviral activity. CS-E inhibited the binding to cells of the purified virus attachment protein gC. A direct interaction of gC with immobilized CS-E and inhibition of this binding by CS-E oligosaccharide fragments greater than octasaccharide were demonstrated. Likewise, the gro2C-specific CS chains interfered with the binding of viral gC to these cells and were found to contain a considerable proportion (13%) of the E-disaccharide unit, suggesting that this unit is an essential component of the CS receptor for herpes simplex virus on gro2C cells and that the antiviral activity of CS-E was due to interference with the binding of viral gC to a CS-E-like receptor on the cell surface. Knowledge of the determinants of antiviral properties of CS-E will help in the development of inhibitors of herpes simplex virus infections in humans.
Keyword
- Animals
- Antiviral Agents
- pharmacology
- Binding Sites
- Cartilage
- metabolism
- Cercopithecus aethiops
- Chondroitin ABC Lyase
- chemistry
- Chondroitin Sulfates
- chemistry
- Decapodiformes
- Disaccharides
- chemistry
- Dose-Response Relationship
- Drug
- Enzyme-Linked Immunosorbent Assay
- Heparitin Sulfate
- chemistry
- Humans
- Inhibitory Concentration 50
- Ligands
- Mice
- Oligosaccharides
- chemistry
- Protein Binding
- Simplexvirus
- metabolism
Publication and Content Type
- ref (subject category)
- art (subject category)
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Bergefall, Kicki ...
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Trybala, Edward, ...
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Johansson, Maria ...
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Uyama, Toru
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Naito, Satomi
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Yamada, Shuhei
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show more...
-
Kitagawa, Hirosh ...
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Sugahara, Kazuyu ...
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Bergström, Tomas ...
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The Journal of b ...
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University of Gothenburg