A novel influenza A virus mitochondrial protein that induces cell death

By Weisan Chen, P. Calvo, D. Malide, J. Gibbs, U. Schubert, I. Bačík, Sameh Basta, R. O'neill, J. Schickli, P. Palese and 3 more. Nature Medicine, 2001

1,088 citations recorded by the source corpus.

Subfields: Epidemiology, Immunology

View Paper: https://www.semanticscholar.org/paper/3771ebc2d175df44f7605293df27a4e83e46764e

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Citations in the corpus

Influenza Research Database: An integrated bioinformatics resource for influenza virus research (2016, background): “In recent years, the influenza community has identified several novel proteins generated from non-canonical translation strategies such as leaky ribosomal scanning (PB1-F2 (10), PB1-N40 (11), PA-N155 (12) and PA-N182 (12)), ribosomal frameshift (PA-X (13)) and alternative splicing (M42 (14) and NS3 ”
An Overlapping Protein-Coding Region in Influenza A Virus Segment 3 Modulates the Host Response (2012, background): “The proteins PB1-N40 (20) and PB1-F2 (21) are also recent discoveries in the IAV proteome, and it is interesting that the X-ORF exhibits greater codon-level conservation than does PB1F2, which is also expressed from an overlapping ORF (10, 22, 23).”
Pushing the limits of the scanning mechanism for initiation of translation (2002, neutral): “For some other viruses, the second protein is a virulence factor that weakens host defenses (Bridgen et al., 2001; Chen et al., 2001; Weber et al., 2002).”
THE BIOLOGY OF INFLUENZA VIRUSES (2008, background): “All influenza viruses encode the polymerase subunit PB1 on segment 2; in some strains of influenza A virus, this segment also codes for the accessory protein PB1-F2, a small, 87-amino acid protein with pro-apoptotic activity, in a +1 alternate reading frame [3].”
Influenza Virus Evolution, Host Adaptation and Pandemic Formation (2010, background): “The PB1-F2 protein encoded from a +1 open reading frame (ORF) within the PB1 ORF (Chen et al., 2001), is highly variable in coding sequence in wild bird IAV (Holmes et al.”
ZBP1/DAI is an innate sensor of influenza virus triggering the NLRP3 inflammasome and programmed cell death pathways (2016, positive): “The interconnected and complimentary nature of IAV-induced cell death pathways demonstrated in our study also helps to explain PB1-F2mediated NLRP3 inflammasome activation since PB1-F2 is regarded as the viral effector mediating cell death in IAV-infected cells (35, 37).”
Mitochondrial membrane permeabilization in cell death. (2007, background): “PB1-F2 has unusual properties compared with other influenza virus proteins, including a peculiar mode of translation, its absence from some animal isolates of the virus, variable expression levels in infected individuals, proteasome-dependent degradation, and mitochondrial localization (116).”
Insights into the Interaction between Influenza Virus and Pneumococcus (2006, background): “Data from our lab suggest that PB1-F2, a recently discovered proapoptotic protein encoded by most human influenza A viruses (19, 50), contributes to this inflammatory response (J.”
Stability-mediated epistasis constrains the evolution of an influenza protein (2013, methodology): “We used lentiviral transduction to create the cell lines 293T-CMV-Nan95-PB1 and MDCK-SIAT1-CMV-Nan95-PB1, which express the coding sequence of the Nanchang/1995 PB1 with the F2 peptide disrupted after its eighth codon (Chen et al., 2001) under control of a CMV promoter.”