ArticleFrontiers in microbiology2018
Amino Acid Substitutions HA A150V, PA A343T, and PB2 E627K Increase the Virulence of H5N6 Influenza Virus in Mice.
Article in Frontiers in microbiology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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17 citing papers in PubMed, 25 citations in OpenAlex.
- Cellular hnRNP AB inhibits avian influenza virus RNA synthesis via blocking UAP56-mediated nuclear export of PB2 mRNA.Veterinary research · 2025Article
- Identification and characterization of a broadly neutralizing and protective nanobody against the HA1 domain of H5 avian influenza virus hemagglutinin.Journal of virology · 2025Article
- Synergistic effects of PA (S184N) and PB2 (E627K) mutations on the increased pathogenicity of H3N2 canine influenza virus infections in mice and dogs.Journal of virology · 2025Article
- Chicken ANP32A-independent replication of highly pathogenic avian influenza viruses potentially leads to mammalian adaptation-related amino acid substitutions in viral PB2 and PA proteins.Journal of virology · 2025Article
- Investigation of human infection with H5N6 avian influenza cases in Sichuan Province from 2014 to 2024: a retrospective study.Frontiers in public health · 2025Article
- Establishment of an infectious clone of the porcine transmissible gastroenteritis virus and a study on the location and function of accessory protein 3.Frontiers in cellular and infection microbiology · 2025Article
- Characterization of H5N1 avian influenza virus isolated from bird in Russia with the E627K mutation in the PB2 protein.Scientific reports · 2024Article
- BAG6 inhibits influenza A virus replication by inducing viral polymerase subunit PB2 degradation and perturbing RdRp complex assembly.PLoS pathogens · 2024Article
- Pathogenicity and virulence of influenza.Virulence · 2023Review
- An Influenza A virus can evolve to use human ANP32E through altering polymerase dimerization.Nature communications · 2023Article
- Highly Pathogenic Avian Influenza H5N1 Virus Infections in Wild Red Foxes (Vulpes vulpes) Show Neurotropism and Adaptive Virus Mutations.Microbiology spectrum · 2023Article
- Zoonotic Mutation of Highly Pathogenic Avian Influenza H5N1 Virus Identified in the Brain of Multiple Wild Carnivore Species.Pathogens (Basel, Switzerland) · 2023Article
- Antigen-capture ELISA and immunochromatographic test strip to detect the H9N2 subtype avian influenza virus rapidly based on monoclonal antibodies.Virology journal · 2021Article
- Genetic diversity, phylogeography, and evolutionary dynamics of highly pathogenic avian influenza A (H5N6) viruses.Virus evolution · 2020Article
- Generation of neutralizing and non-neutralizing monoclonal antibodies against H7N9 influenza virus.Emerging microbes & infections · 2020Article
- Structures of influenza A virus RNA polymerase offer insight into viral genome replication.Nature · 2019Article
- Multiple amino acid substitutions involved in the adaption of three avian-origin H7N9 influenza viruses in mice.Virology journal · 2019Article
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11 authors at 2 institutions in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
H5N6 avian influenza viruses (AIVs) can cause severe pneumonia and death in humans. However, the molecular determinants of H5N6 influenza virus mammalian adaption are still unclear. Three amino acid substitutions (HA A150V, PA A343T, PB2 E627K) are observed in H5N6 virus A/duck/Zhejiang/6D2/2013 (6D2) in lung-to-lung passage in mice. These substitutions are crucial to the pathogenicity of mouse-adapted virus. In this study, we investigated the contribution of each amino acid substitution in the virus by reverse genetics. The results demonstrate that HA A150V greatly altered the receptor binding preference of 6D2. Virus bearing this substitution acquired increased mortality than mice infected with wild-type 6D2. The PA A343T substitution mildly enhanced viral polymerase activity but the reduced survival rate in mice indicates this substitution may change the immunoreaction of the host. The well-known PB2 E627K substitution increased eight folds the relative polymerase activity compared to PA A343T and resulted in 100% death rate in mice. In addition, we show that PA A343T dramatically exacerbates the effect of PB2 E627K on viral polymerase activity; when combined, these two substitutions work synergistically. However, HA A150V and PA A343T seemed to attenuate PB2 E627K
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