ArticleThe Journal of biological chemistry2016
Amyloid Assemblies of Influenza A Virus PB1-F2 Protein Damage Membrane and Induce Cytotoxicity.
Article in The Journal of biological chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.
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Who cites it
32 citing papers in PubMed, 74 citations in OpenAlex.
- Poultry handling-related stress alters membrane composition, extracellular vesicle production, survival, and virulence inApplied and environmental microbiology · 2026Article
- Genetic Determinants Analysis of PB1 and PB2 Genes in H5N1 Avian Influenza Strains from Romania.Pathogens (Basel, Switzerland) · 2026Article
- Computational Insights into PB1-F2 Mediated Modulation of VDAC1: An Allosteric Mechanism in Mitochondrial Dysfunction.ACS omega · 2026Article
- Predicting Peptide Aggregation with Protein Language Model Embeddings.Journal of chemical information and modeling · 2026Article
- Dissecting Cell Death Pathways in Influenza A Virus Infection: Comparative Insights from Human Models.Viruses · 2026Review
- Genomic characterization of equine influenza A subtype H3N8 viruses by long read sequencing and functional analyses of the PB1-F2 virulence factor of A/equine/Paris/1/2018.Veterinary research · 2024Article
- Article
- Synthetic Cell Lines for Inducible Packaging of Influenza A Virus.ACS synthetic biology · 2024Article
- Low complexity domains of the nucleocapsid protein of SARS-CoV-2 form amyloid fibrils.Nature communications · 2023Article
- Peptide from NSP7 is able to form amyloid-like fibrils: Artifact or challenge to drug design?Biochimica et biophysica acta. Proteins and proteomics · 2023Article
- Comparison of PB1-F2 Proximity Interactomes Reveals Functional Differences between a Human and an Avian Influenza Virus.Viruses · 2023Article
- Investigating the Role of African Horse Sickness Virus VP7 Protein Crystalline Particles on Virus Replication and Release.Viruses · 2022Article
- PB1F2 from Influenza A Virus Regulates the Interaction between Cytochrome C and Cardiolipin.Membranes · 2022Article
- Generation of a Soluble African Horse Sickness Virus VP7 Protein Capable of Forming Core-like Particles.Viruses · 2022Article
- The Roles of Ubiquitination in Pathogenesis of Influenza Virus Infection.International journal of molecular sciences · 2022Review
- Experimental Evidence of Intrinsic Disorder and Amyloid Formation by theInternational journal of molecular sciences · 2022Article
- Study of the host specificity of PB1-F2-associated virulence.Virulence · 2021Article
- Identification of a Region in the Common Amino-terminal Domain of Hendra Virus P, V, and W Proteins Responsible for Phase Transition and Amyloid Formation.Biomolecules · 2021Article
- Viral Induced Protein Aggregation: A Mechanism of Immune Evasion.International journal of molecular sciences · 2021Review
- Influenza A viruses limit NLRP3-NEK7-complex formation and pyroptosis in human macrophages.EMBO reports · 2020Article
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Authors and funding
8 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
PB1-F2 is a small accessory protein encoded by an alternative open reading frame in PB1 segments of most influenza A virus. PB1-F2 is involved in virulence by inducing mitochondria-mediated immune cells apoptosis, increasing inflammation, and enhancing predisposition to secondary bacterial infections. Using biophysical approaches we characterized membrane disruptive activity of the full-length PB1-F2 (90 amino acids), its N-terminal domain (52 amino acids), expressed by currently circulating H1N1 viruses, and its C-terminal domain (38 amino acids). Both full-length and N-terminal domain of PB1-F2 are soluble at pH values ≤6, whereas the C-terminal fragment was found soluble only at pH ≤ 3. All three peptides are intrinsically disordered. At pH ≥ 7, the C-terminal part of PB1-F2 spontaneously switches to amyloid oligomers, whereas full-length and the N-terminal domain of PB1-F2 aggregate to amorphous structures. When incubated with anionic liposomes at pH 5, full-length and the C-terminal part of PB1-F2 assemble into amyloid structures and disrupt membrane at nanomolar concentrations. PB1-F2 and its C-terminal exhibit no significant antimicrobial activity. When added in the culture medium of mammalian cells, PB1-F2 amorphous aggregates show no cytotoxicity, whereas PB1-F2 pre-assembled into amyloid oligomers or fragmented nanoscaled fibrils was highly cytotoxic. Furthermore, the formation of PB1-F2 amyloid oligomers in infected cells was directly reflected by membrane disruption and cell death as observed in U937 and A549 cells. Altogether our results demonstrate that membrane-lytic activity of PB1-F2 is closely linked to supramolecular organization of the protein.
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