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Basic Characteristics of Mutations
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Mutation Site
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P200S |
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Mutation Site Sentence
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Three of the mutations (P200S and S202T close to the 190 alpha helix, and I233T along the 220 loop) were in close proximity to the receptor-binding domain (Fig 1B). |
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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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HA1 |
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Standardized Encoding Gene
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HA
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Genotype/Subtype
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H1N1 |
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Viral Reference
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JF915184.1
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Functional Impact and Mechanisms
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Disease
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Influenza A
Influenza B
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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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- |
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Treatment
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- |
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Location
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America |
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Literature Information
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PMID
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29145498
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Title
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Antigenicity of the 2015-2016 seasonal H1N1 human influenza virus HA and NA proteins
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Author
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Clark AM,DeDiego ML,Anderson CS,Wang J,Yang H,Nogales A,Martinez-Sobrido L,Zand MS,Sangster MY,Topham DJ
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Journal
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PloS one
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Journal Info
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2017 Nov 16;12(11):e0188267
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Abstract
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Antigenic drift of the hemagglutinin (HA) and neuraminidase (NA) influenza virus proteins contributes to reduced vaccine efficacy. To analyze antigenic drift in human seasonal H1N1 viruses derived from the 2009 pandemic H1N1 virus (pH1N1-like viruses) accounts for the limited effectiveness (around 40%) of vaccination against pH1N1-like viruses during the 2015-2016 season, nasal washes/swabs collected from adult subjects in the Rochester, NY area, were used to sequence and isolate the circulating viruses. The HA and NA proteins from viruses circulating during the 2015-2016 season encoded eighteen and fourteen amino acid differences, respectively, when compared to A/California/04/2009, a strain circulating at the origin of the 2009 pandemic. The circulating strains belonged to subclade 6B.1, defined by HA amino acid substitutions S101N, S179N, and I233T. Hemagglutination-inhibiting (HAI) and HA-specific neutralizing serum antibody (Ab) titers from around 50% of pH1N1-like virus-infected subjects and immune ferrets were 2-4 fold lower for the 2015-2016 circulating strains compared to the vaccine strain. In addition, using a luminex-based mPlex HA assay, the binding of human sera from subjects infected with pH1N1-like viruses to the HA proteins from circulating and vaccine strains was not identical, strongly suggesting antigenic differences in the HA protein. Additionally, NA inhibition (NAI) Ab titers in human sera from pH1N1-like virus-infected subjects increased after the infection and there were measurable antigenic differences between the NA protein of circulating strains and the vaccine strain using both ferret and human antisera. Despite having been vaccinated, infected subjects exhibited low HAI Ab titers against the vaccine and circulating strains. This suggests that poor responses to the H1N1 component of the vaccine as well as antigenic differences in the HA and NA proteins of currently circulating pH1N1-like viruses could be contributing to risk of infection even after vaccination.
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Sequence Data
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-
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