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Basic Characteristics of Mutations
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Mutation Site
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L226Q |
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Mutation Site Sentence
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Four HA changes, S133N, T189A, N198D, and L226Q, were associated with a significant increase in HA thermostability compared to the wild-type virus. |
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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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HA |
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Standardized Encoding Gene
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HA
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Genotype/Subtype
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H9N2 |
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Viral Reference
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AF222810
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Functional Impact and Mechanisms
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Disease
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Influenza A
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Immune
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- |
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Target Gene
|
-
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Clinical and Epidemiological Correlations
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Clinical Information
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- |
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Treatment
|
- |
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Location
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HongKong |
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Literature Information
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PMID
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27586413
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Title
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Effects of hemagglutinin amino acid substitutions in H9 influenza A virus escape mutants
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Author
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Rudneva IA,Timofeeva TA,Ignatieva AV,Shilov AA,Ilyushina NA
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Journal
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Archives of virology
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Journal Info
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2016 Dec;161(12):3515-3520
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Abstract
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We assessed the pH optimum of fusion, HA thermostability, and in vitro replication kinetics of previously obtained influenza H9 escape mutants. The N198S mutation significantly increased the optimum pH of fusion. Four HA changes, S133N, T189A, N198D, and L226Q, were associated with a significant increase in HA thermostability compared to the wild-type virus. HA amino acid changes at positions 116, 133, 135, 157, 162, and 193 significantly decreased the replicative ability of H9 escape mutants in vitro. Monitoring of pleiotropic effects of the HA mutations found in H9 escape mutants is essential for accurate prediction of all possible outcomes of immune selection of H9 influenza A viruses.
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Sequence Data
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AY428285
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