Detection of haemagglutinin D222 polymorphisms in influenza A(H1N1)pdm09-infected patients by ultra-deep pyrosequencing.
PMID: 22862843
2013
Clinical microbiology and infection
Abstract: D222E, D222G, D222N and D222A were observed in 37.0%, 11.1%, 7.4% and 3.7% of patients, respectively; 10.7% of samples harboured more than two variants.
Abstract: D222G/N/A were detected, as either minor or predominant variants, only in severe cases, whereas D222E was equally represented in severe and moderate-mild infections.
Molecular and serological investigations of the Influenza A(H1N1) 2009 pandemic virus in Turkey.
PMID: 23483248
2013
Medical microbiology and immunology
Abstract: D222G was detected in nasal samples from two severe cases.
Abstract: Thirteen rRT-PCR positive samples were analyzed for presence of mutations that have been associated with host range, virulence, and antiviral resistance: substitution D222G in the HA, E627K in the PB2, and H275Y in the neuraminidase (NA).
Analysis of adaptation mutants in the hemagglutinin of the influenza A(H1N1)pdm09 virus.
Introduction: D222G has also been shown to be associated with increased virulence, though other groups have not seen this association .
Introduction: An example of one such mutation that has been studied fairly thoroughly is the D222G mutation which has been shown to alter receptor specificity and tropism.
Discussion: Consistent with our results, mutation D222G possesses increased affinity for alpha2,6 receptors compared with D222.
Discussion: In the case of variant 3, polymorphism at position 222 has been extensively studied due mainly to mutation D222G, which has been associated with severe influenza as a consequence of change in the preference of sialic acid receptors.
Evaluation of HA-D222G/N polymorphism using targeted NGS analysis in A(H1N1)pdm09 influenza virus in Russia in 2018-2019.
Discussion: (2010) and, since then, different studies in several countries have found the D222G substitution to be more frequently associated with patients with severe pandemic influenza than in non-severe control cases.
Discussion: Although most of studies demonstrated the presence of D222G substitution in severe cases, it was also reported in mild cases.
Discussion: Although, 7% of them, found in severe cases in the present study, had the D222G substitution.
Discussion: An association between D222G and severity was initially proposed by Kilander et al.
Discussion: Further study is warranted to elucidate the intriguing relationship between D222G substitution and severe disease.
Discussion: It is worth noting that although the Asp222Gly mutation cu
Acute respiratory distress syndrome induced by a swine 2009 H1N1 variant in mice.
Introduction: In the present study, we used a virulent variant 2009 H1N1 virus, which was isolated from a pig and possessed a virulence-associated HA-D222G mutation, to establish an ARDS mouse model.
Discussion: It has been shown that 2009 H1N1 virus possessing a D222G mutation in hemagglutinin (HA) could increase the pathogenicity in mice and binding to the alpha-2,3 SA receptor.
Discussion: Notably, the swine isolate, SD/09, had a D222G mutation in HA.
Discussion: Therefore, we suggest that the variant possessing the D222G mutation in HA can induce PMID: 21874012
2012
Modern pathology
Abstract: In addition, the D222G amino acid substitution in influenza virus hemagglutinin, which binds to specific cell receptors, was analyzed in formalin-fixed and paraffin-embedded trachea and lung sections by direct sequencing of PCR-amplified products.
Abstract: In one case, the D222G substitution was detected in the lung as a major sequence, although 222D was prominent in the trachea, suggesting that selection of the viral clones occurred in the respiratory tract.
Emergence of HA mutants during influenza virus pneumonia.
PMID: 23071861
2012
International journal of clinical and experimental pathology
Abstract: An infection model utilizing guinea pigs, which was chosen in order to best simulate the sialic acid distribution of severe pneumonia in human patients, demonstrated an increase of D222G mutants and a delay in the diminution of mutants in the lower respiratory tract in comparison to the upper respiratory tract.
Abstract: Mutations at amino acid 222 (D222G mutations) in the virus hemagglutinin (HA) molecule, known to alter the receptor-recognition properties of the virus, were detected in a number of the more severely-affected patients in the early phases of the pandemic.
Abstract: To understand the background for the emergence of the mutant amino acid D222G in human lungs, we conducted histological examinations on lung specimens of patients from Mexico who h
Treatment of oseltamivir-resistant influenza A (H1N1) virus infections in mice with antiviral agents.
Introduction: The influenza A/California/04/2009 (H1N1) virus that was mouse adapted had the following mutations compared to wild-type virus: 1 in PB2 (E158G), 3 in HA (G155E, S183P, and D222G), and 1 in NP (D101G) genes.
Both influenza hemagglutinin and polymerase acidic genes are important for delayed pandemic 2009 H1N1 virus clearance in the ferret model.
Result: HA K119N, G155E, S183P, R221K, D222G, and D225G lead to increased virulence in mice.
Result: HA D222G altered the receptor binding properties of the virus, and PA F35L increased its polymerase activity; the mutant virus was therefore similar to our G1 or HAmutPAmut strain.
Result: However, a synergistic role of influenza HA and PA proteins has recently been reported with HA D222G, HA
Evaluation of HA-D222G/N polymorphism using targeted NGS analysis in A(H1N1)pdm09 influenza virus in Russia in 2018-2019.
Abstract: D222G mutation of the hemagglutinin (HA) is of special interest because of its close association with the enhanced virulence of 2009 pandemic influenza A (H1N1) virus through the increased binding affinity to alpha2,3-linked sialylated glycan receptors.
Abstract: Here, molecular dynamics simulation and binding free energy calculation were performed to explore the altered glycan receptor binding mechanism of HA upon the D222G mutation by studying the interaction of one alpha2,3-linked sialylglycan (sequence: SIA-GAL-NAG) with the wild type and D222G mutated HA.
Abstract: The binding free energy calculation based on the molecular mechanics generalized Born surface area (MM-GBSA) method indicates that the
ViMRT
IV mutation literature information.
PMID: 
2013
Clinical microbiology and infection
