1uzg
From Proteopedia
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==Overview== | ==Overview== | ||
| - | Dengue virus is an emerging global health threat. The major envelope | + | Dengue virus is an emerging global health threat. The major envelope glycoprotein, E, mediates viral attachment and entry by membrane fusion. Antibodies that bind but fail to neutralize noncognate serotypes enhance infection. We have determined the crystal structure of a soluble fragment of the envelope glycoprotein E from dengue virus type 3. The structure closely resembles those of E proteins from dengue type 2 and tick-borne encephalitis viruses. Serotype-specific neutralization escape mutants in dengue virus E proteins are all located on a surface of domain III, which has been implicated in receptor binding. While antibodies against epitopes in domain I are nonneutralizing in dengue virus, there are neutralizing antibodies that recognize serotype-conserved epitopes in domain II. The mechanism of neutralization for these antibodies is probably inhibition of membrane fusion. Our structure shows that neighboring glycans on the viral surface are spaced widely enough (at least 32 A) that they can interact with multiple carbohydrate recognition domains on oligomeric lectins such as DC-SIGN, ensuring maximum affinity for these putative receptors. |
==About this Structure== | ==About this Structure== | ||
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[[Category: Dengue virus type 1]] | [[Category: Dengue virus type 1]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Harrison, S | + | [[Category: Harrison, S C.]] |
[[Category: Modis, Y.]] | [[Category: Modis, Y.]] | ||
[[Category: BMA]] | [[Category: BMA]] | ||
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[[Category: virus/viral protein]] | [[Category: virus/viral protein]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:30:03 2008'' |
Revision as of 13:30, 21 February 2008
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CRYSTAL STRUCTURE OF THE DENGUE TYPE 3 VIRUS ENVELOPE PROTEIN
Overview
Dengue virus is an emerging global health threat. The major envelope glycoprotein, E, mediates viral attachment and entry by membrane fusion. Antibodies that bind but fail to neutralize noncognate serotypes enhance infection. We have determined the crystal structure of a soluble fragment of the envelope glycoprotein E from dengue virus type 3. The structure closely resembles those of E proteins from dengue type 2 and tick-borne encephalitis viruses. Serotype-specific neutralization escape mutants in dengue virus E proteins are all located on a surface of domain III, which has been implicated in receptor binding. While antibodies against epitopes in domain I are nonneutralizing in dengue virus, there are neutralizing antibodies that recognize serotype-conserved epitopes in domain II. The mechanism of neutralization for these antibodies is probably inhibition of membrane fusion. Our structure shows that neighboring glycans on the viral surface are spaced widely enough (at least 32 A) that they can interact with multiple carbohydrate recognition domains on oligomeric lectins such as DC-SIGN, ensuring maximum affinity for these putative receptors.
About this Structure
1UZG is a Single protein structure of sequence from Dengue virus type 1 with , and as ligands. Known structural/functional Site: . Full crystallographic information is available from OCA.
Reference
Variable surface epitopes in the crystal structure of dengue virus type 3 envelope glycoprotein., Modis Y, Ogata S, Clements D, Harrison SC, J Virol. 2005 Jan;79(2):1223-31. PMID:15613349
Page seeded by OCA on Thu Feb 21 15:30:03 2008
Categories: Dengue virus type 1 | Single protein | Harrison, S C. | Modis, Y. | BMA | FUL | NAG | Atp-binding | Class 2 fusion protein | Dengue virus | Envelope protein | Flavivirus | Fusion loop | Glycoprotein | Helicase | Hydrolase | Membrane fusion | Nonstructural protein | Polyprotein | Rna-directed rna polymerase | Transferase | Transmembrane | Virus/viral protein
