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Basic Characteristics of Mutations
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Mutation Site
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N67D |
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Mutation Site Sentence
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Sequencing the structural proteins of HHA(res) resulted in two mutations, N67D and T155I, indicating a deletion of both N-glycosylation sites on the viral envelope E-glycoprotein. |
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Mutation Level
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Amino acid level |
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Mutation Type
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Nonsynonymous substitution |
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Gene/Protein/Region
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E |
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Standardized Encoding Gene
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Envelope
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Genotype/Subtype
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DENV-2 |
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Viral Reference
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M29095
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Functional Impact and Mechanisms
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Disease
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Cell line
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Immune
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- |
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Target Gene
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CD209
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Clinical and Epidemiological Correlations
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Clinical Information
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- |
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Treatment
|
Hippeastrum hybrid agglutinin (HHA) |
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Location
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- |
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Literature Information
|
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PMID
|
23124109
|
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Title
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Crucial role of the N-glycans on the viral E-envelope glycoprotein in DC-SIGN-mediated dengue virus infection
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Author
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Alen MM,Dallmeier K,Balzarini J,Neyts J,Schols D
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Journal
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Antiviral research
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Journal Info
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2012 Dec;96(3):280-7
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Abstract
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We generated in the mosquito cell line C6/36 a dengue virus (DENV) resistant to Hippeastrum hybrid agglutinin (HHA), a carbohydrate-binding agent (CBA). The genotype and phenotype were characterized of the HHA resistant (HHA(res)) DENV compared to the wild-type (WT) DENV. Sequencing the structural proteins of HHA(res) resulted in two mutations, N67D and T155I, indicating a deletion of both N-glycosylation sites on the viral envelope E-glycoprotein. The HHA(res) DENV could replicate in mammalian and mosquito cells that are lacking dendritic cell-specific intercellular adhesion molecule 3-grabbing non-integrin (DC-SIGN) expression. In contrast, DC-SIGN expressing human cells namely monocyte-derived dendritic cells as well as DC-SIGN-transfected cells were no longer susceptible to HHA(res) DENV. This demonstrates a crucial role of the N-glycans in the E-glycoprotein in the infection of dendritic cells, which constitute primary target cells of DENV during viral pathogenesis in the human body.
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Sequence Data
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-
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