Publications by authors named "Eileigh Kadijk"
Many viruses inhibit general host gene expression to limit innate immune responses and gain preferential access to the cellular translational apparatus for their protein synthesis. This process is known as host shutoff. Influenza A viruses (IAVs) encode two host shutoff proteins: nonstructural protein 1 (NS1) and polymerase acidic X (PA-X).
View Article and Find Full Text PDFProximity-dependent biotinylation (PDB) techniques provide information about the molecular neighborhood of a protein of interest, yielding insights into its function and localization. Here, we assessed how different labeling enzymes and streptavidin resins influence PDB results. We compared the high-confidence interactors of the DNA/RNA-binding protein transactive response DNA-binding protein 43 kDa (TDP-43) identified using either miniTurbo (biotin ligase) or APEX2 (peroxidase) enzymes.
View Article and Find Full Text PDFArticle Synopsis
- Influenza A viruses (IAVs) manipulate host cellular mechanisms to evade antiviral responses and enhance viral protein production, particularly affecting the translation process in infected cells.
- The study identified two thiopurines, 6-thioguanine (6-TG) and 6-thioguanosine (6-TGo), which can induce the formation of stress granules and inhibit IAV replication specifically by disrupting the synthesis of key glycoproteins, hemagglutinin (HA) and neuraminidase (NA), without affecting other viral proteins.
- The activation of the unfolded protein response (UPR) emerged as a significant factor in this process, with the study suggesting that manipulating UPR pathways could enhance