ArticleJournal of virology2011
Targeting of the influenza A virus polymerase PB1-PB2 interface indicates strain-specific assembly differences.
Article in Journal of virology, 2011. 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.
- PB1 mutations as key drivers of influenza A virus evolution.Frontiers in microbiology · 2026Review
- Cryptic proteins translated from deletion-containing viral genomes dramatically expand the influenza virus proteome.Nucleic acids research · 2024Article
- Cryptic proteins translated from deletion-containing viral genomes dramatically expand the influenza virus proteome.bioRxiv : the preprint server for biology · 2024Article
- The ubiquitination landscape of the influenza A virus polymerase.Nature communications · 2023Article
- Molecular Docking and Virtual Screening of an Influenza Virus Inhibitor That Disrupts Protein-Protein Interactions.Viruses · 2021Article
- Inhibition of Influenza Virus Polymerase by Interfering with Its Protein-Protein Interactions.ACS infectious diseases · 2021Review
- Discovery of anti-influenza nucleoside triphosphates targeting the catalytic site of A/PR/8/34/H1N1 polymerase.Medicinal chemistry research : an international journal for rapid communications on design and mechanisms of action of biologically active agents · 2020Article
- Eurasian Avian-Like Swine Influenza A Viruses Escape Human MxA Restriction through Distinct Mutations in Their NucleoproteinJournal of virology · 2019Article
- Comparative influenza protein interactomes identify the role of plakophilin 2 in virus restriction.Nature communications · 2017Article
- Identification of a novel small-molecule compound targeting the influenza A virus polymerase PB1-PB2 interface.Antiviral research · 2017Article
- The Influenza Virus Polymerase Complex: An Update on Its Structure, Functions, and Significance for Antiviral Drug Design.Medicinal research reviews · 2016Review
- TRIM32 Senses and Restricts Influenza A Virus by Ubiquitination of PB1 Polymerase.PLoS pathogens · 2015Article
- Article
- Pandemic influenza A viruses escape from restriction by human MxA through adaptive mutations in the nucleoprotein.PLoS pathogens · 2013Article
- Adaptive mutations in NEP compensate for defective H5N1 RNA replication in cultured human cells.Nature communications · 2012Article
- Small molecule inhibitors of influenza A and B viruses that act by disrupting subunit interactions of the viral polymerase.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
Corrections and comments
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Authors and funding
5 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Assembly of the heterotrimeric influenza virus polymerase complex from the individual subunits PB1, PA, and PB2 is a prerequisite for viral replication. The conserved protein-protein interaction sites have been suggested as potential drug targets. To characterize the PB1-PB2 interface, we fused the PB1-binding domain of PB2 to green fluorescent protein (PB2(1-37)-GFP) and determined its competitive inhibitory effect on the polymerase activity of influenza A virus strains. Coexpression of PB2(1-37)-GFP in a polymerase reconstitution system led to substantial inhibition of the polymerase of A/WSN/33 (H1N1). Surprisingly, polymerases of other strains, including A/SC35M (H7N7), A/Puerto Rico/8/34 (H1N1), A/Hamburg/4/2009 (H1N1), and A/Thailand/1(KAN-1)/2004 (H5N1), showed various degrees of resistance. Individual exchange of polymerase subunits and the nucleoprotein between the sensitive WSN polymerase and the insensitive SC35M polymerase mapped the resistance to both PB1 and PA of SC35M polymerase. While PB2(1-37)-GFP bound equally well to the PB1 subunits of both virus strains, PB1-PA dimers of SC35M polymerase showed impaired binding compared to PB1-PA dimers of WSN polymerase. The use of PA(SC35M/WSN) chimeras revealed that the reduced affinity of the SC35M PB1-PA dimer was mediated by the N-terminal 277 amino acids of PA. Based on these observations, we speculate that the PB1-PA dimer formation of resistant polymerases shields the PB2(1-37) binding site, whereas sensitive polymerases allow this interaction, suggesting different assembly strategies of the trimeric polymerase complex between different influenza A virus strains.
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