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Basic Characteristics of Mutations
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Mutation Site
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D253N |
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Mutation Site Sentence
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Virus with PB2 D253N and Q591K had greater polymerase activity in minireplicon assays, induced more tumor necrosis factor alpha (TNF-alpha) in human macrophages, replicated better in differentiated normal human bronchial epithelial (NHBE) cells, and was more pathogenic for mice. |
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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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PB2 |
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Standardized Encoding Gene
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PB2
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Genotype/Subtype
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H9N2 |
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Viral Reference
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-
|
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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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-
|
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Clinical and Epidemiological Correlations
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Clinical Information
|
- |
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Treatment
|
- |
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Location
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- |
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Literature Information
|
|
PMID
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21734052
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Title
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Amino acid residues 253 and 591 of the PB2 protein of avian influenza virus A H9N2 contribute to mammalian pathogenesis
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Author
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Mok CK,Yen HL,Yu MY,Yuen KM,Sia SF,Chan MC,Qin G,Tu WW,Peiris JS
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Journal
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Journal of virology
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Journal Info
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2011 Sep;85(18):9641-5
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Abstract
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We investigated the tropism, host responses, and virulence of two variants of A/Quail/Hong Kong/G1/1997 (H9N2) (H9N2/G1) with D253N and Q591K in the PB2 protein in primary human macrophages and bronchial epithelium in vitro and in mice in vivo. Virus with PB2 D253N and Q591K had greater polymerase activity in minireplicon assays, induced more tumor necrosis factor alpha (TNF-alpha) in human macrophages, replicated better in differentiated normal human bronchial epithelial (NHBE) cells, and was more pathogenic for mice. Taken together, our studies help define the viral genetic determinants that contribute to pathogenicity of H9N2 viruses.
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Sequence Data
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-
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