Amino acid changes in HA and determinants of pathogenicity associated with influenza virus A H1N1pdm09 during the winter seasons 2015-2016 and 2016-2017 in Mexico.
Abstract: We also found the D222 G substitution, which has been associated with a higher tropism towards the lower respiratory tract, and a non-reported insertion of one Ile in NS1 (Ile113).
Influenza A virus hemagglutinin mutations associated with use of neuraminidase inhibitors correlate with decreased inhibition by anti-influenza antibodies.
Discussion: Consistent with the previous reports, our data showed that recombinant virus containing D222G resulted in ~ 2 log10PFU/mL higher titers over 72 h of replication in cell culture.
Discussion: In addition, S183P and D222G altered receptor binding avidity of the A/Puerto Rico/8/34 (H1N1) strain; however, whether a specific mutation results in increased or decreased receptor binding avidity depends on its genetic context.
Discussion: Subjects with the HA1 D222G mutation had significantly longer ICU stays: 22.8 days vs 14.0 days for those without this substitution.
Discussion: The D222G mutation, which maps to the antigenic site Ca, was shown to be closely associated with the enhanced virulence of A(H1N1)pdm09 virus through the increased binding affinity
Amino acid substitutions in low pathogenic avian influenza virus strains isolated from wild birds in Korea.
Abstract: We found substitution rates of 71.7% at the C38Y amino acid site within the polymerase basic protein 1 (PB1) gene, 66.7% at the D222G site within the hemagglutinin (HA) 1 gene, and 75.6% at the A184 site within the nucleoprotein (NP) gene.
Adaptive Mutations in Influenza A/California/07/2009 Enhance Polymerase Activity and Infectious Virion Production.
Result: Of these substitutions, D222G has been found previously in the two CA/04 mouse adaptation studies and is believed to be responsible for increased binding to alpha 2,3-linked sialic acid.
Result: We identified three amino acid substitutions in HA that reached >99% frequency in the CA/07-MA strain: N156D, S183P and D222G (Figure 2 and Table S2).
Discussion: A single amino acid substitution D222G was shown to increase binding of HA to alpha 2,3-sialic acid, and we identified this mutation in our CA/07-MA virus.
Discussion: Namely, the HA substitutions D222G (at 53.9% frequency, Table S2), S183P (22.8%) and PMID: 28132927
2017
Infection, genetics and evolution
Discussion: D222G substitution was shown to cause a shift from alpha2,6-sialic acid receptor specificity to mixed alpha2,3/alpha2,6-sialic acid receptor specificity, adduced thereby to facilitate lung infection.
Discussion: None of the studied viruses carried HA1 D222G/N/S or Q293H substitutions, reported to be found more frequently in patients with severe disease or fatal outcome earlier in the pandemic period.
Pulmonary changes in Norwegian fatal cases of pandemic influenza H1N1 (2009) infection: a morphologic and molecular genetic study.
PMID: 27413002
2016
Influenza and other respiratory viruses
Discussion: In conclusion, our results show a possible association in fatal Norwegian cases from the A(H1N1)pdm09 pandemic between mortality and the factors obesity, underlying illness, and the viral mutation HA D222G.
Discussion: Since the outbreak of the novel A(H1N1)pdm09, post-pandemic studies have described the clinical aspects of this virus.23, 24, 25 Several host factors and underlying conditions have been associated with disease severity.9, 14, 15, 16, 20, 21, 22 These include pneumonia, obesity, pregnancy, in addition to effects of vaccines and neuraminidase inhibitors that were used during the pandemic.23, 24, 25 Kilander et al.29 reported a novel mutation in the major surface glycoprotein HA) of A(H1N1)pdm09, namely HA D222G
In-Depth Analysis of HA and NS1 Genes in A(H1N1)pdm09 Infected Patients.
Discussion: Besides the predominant HA variants S203T and D222E, we detected a number of minority variants (S203P/A, D222G, Q223R and E224G) within the RBS, all reported at low frequency, in the population database (S1 Table).
Analysis of the Contrasting Pathogenicities Induced by the D222G Mutation in 1918 and 2009 Pandemic Influenza A Viruses.
PMID: 26321885
2015
Journal of chemical theory and computation
Abstract: Accumulated mutations at positions 183 and 224 that alter the size of the binding pocket are identified with the fitness of the 2009 pandemic virus carrying the D222G mutation.
Abstract: In 2009, the D222G mutation in the hemagglutinin (HA) glycoprotein of pandemic H1N1 influenza A virus was found to correlate with fatal and severe human infections.
Virological characterization of influenza H1N1pdm09 in Vietnam, 2010-2013.
PMID: 25966032
2015
Influenza and other respiratory viruses
Discussion: However, in early 2011, the D222N substitution was found in three cases in the United States and may correlate with severe clinical manifestations, similar to D222G.
Discussion: Similar to the D222G mutation, the variants D222A, D222E, and D222N also result in enhanced binding to receptor (alpha2-3) of epithelial cells in the lower respiratory tract, whereas wild-type seasonal influenza strains bind preferentially to the alpha2-6 receptor of the upper airway cells.
Discussion: The D222G mutation in the HA of A/H1N1pdm/09 viruses was first reported in Norway in November 2009, raising a possible link between this mutation and greater virulence.
Discussion: The frequency of PMID: 26056814
2015
Molecules (Basel, Switzerland)
Result: The World Health Organisation (WHO) reported that the overall prevalence of the D222G was <1.8% and ~7.1% in fatal cases of H1N1.
IV mutation literature information.
PMID: 
2019
Virus research
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