ArticleVirology2014
Influenza A viruses with different amino acid residues at PB2-627 display distinct replication properties in vitro and in vivo: revealing the sequence plasticity of PB2-627 position.
Article in Virology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 27 citations in OpenAlex.
- An emerging PB2-627 polymorphism increases the zoonotic risk of avian influenza virus by overcoming ANP32 host restriction in mammalian and avian hosts.Journal of virology · 2025Article
- E627V mutation in PB2 protein promotes the mammalian adaptation of novel H10N3 avian influenza virus.Veterinary research · 2025Article
- Exploring the alternative virulence determinants PB2 S155N and PA S49Y/D347G that promote mammalian adaptation of the H9N2 avian influenza virus in mice.Veterinary research · 2023Article
- Comparative analysis of PB2 residue 627E/K/V in H5 subtypes of avian influenza viruses isolated from birds and mammals.Frontiers in veterinary science · 2023Article
- The Species-Specific 282 Residue in the PB2 Subunit of the Polymerase Regulates RNA Synthesis and Replication of Influenza A Viruses Infecting Bat and Nonbat Hosts.Journal of virology · 2022Article
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- Viral Subpopulation Screening Guides in Designing a High Interferon-Inducing Live Attenuated Influenza Vaccine by Targeting Rare Mutations in NS1 and PB2 Proteins.Journal of virology · 2020Article
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- Comprehensive mapping of adaptation of the avian influenza polymerase protein PB2 to humans.eLife · 2019Article
- Characterization of influenza A viruses with polymorphism in PB2 residues 701 and 702.Scientific reports · 2017Article
- Prerequisites for the acquisition of mammalian pathogenicity by influenza A virus with a prototypic avian PB2 gene.Scientific reports · 2017Article
- Recombinant influenza virus with a pandemic H2N2 polymerase complex has a higher adaptive potential than one with seasonal H2N2 polymerase complex.The Journal of general virology · 2016Article
- Transmission of H7N9 Influenza Viruses with a Polymorphism at PB2 Residue 627 in Chickens and Ferrets.Journal of virology · 2015Article
- Identification of mammalian-adapting mutations in the polymerase complex of an avian H5N1 influenza virus.Nature communications · 2015Article
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
Abstract
Sequence analyses of influenza PB2 sequences indicate that the 627 position almost exclusively contains either lysine (K) or glutamic acid (E), suggesting a high sequence constraint at this genetic marker. Here, we used a site-directed random mutagenesis method to demonstrate that PB2-627 position has a high sequence plasticity. Recombinant viruses carrying various amino acid residues at this position are viable in cell cultures. These PB2-627 mutants showed various polymerase activities and replication kinetics in mammalian and avian cells as well as pathogenicity in mice. Serially passaging these mutants in MDCK cells generated some compensatory PB2 mutations that can restore polymerase activities of the PB2-627 mutants. Of these, PB2-D309N was identified as a novel one. Besides showing that influenza virus can tolerate a wide range of amino acid residues at the PB2-627 position, this study also demonstrates a potential strategy to identify novel mutations that can enhance viral polymerase.
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