How does a virus stress a cell? When a virus infects a eukaryotic cell, most cells activate a cellular stress response. This response protects cells against several different types of stress such as heat and osmotic shock, but has lately been found to be triggered by many viruses as well. During stress, the cell stalls nearly all protein synthesis and promotes only translation of proteins important for cell homeostasis. The stalled translation initiation complexes are stored in cytoplas-mic 48 stress granules (SGs), but can then quickly be released when the stress has been lifted. This reprogramming of host gene expression is often to the disadvantage for viruses, who are heavily dependent on the host cell machinery. Consequently, many viruses target the stress response (of-ten the formation of SGs) to be able to establish a productive infection. This further suggests that SGs are ancient and crucial components of the first line of defense against viruses and something the virus has to confront. We have recently identified a viral protein (from the foot-and-mouth disease virus) that cleaves one of the key components of SGs. This cleavage leads to impaired SGs formation in infected cells. The aim of this project is to determine how the virus disrupts the SGs and to further investigate how these granules are formed. The results will provide valuable information on the host - virus interplay and the cellular defense against pathogens. Techniques used in the project: - PCR - Cloning - Sequencing - Protein expression and purification - Cell culturing and transfection - Microscopy ECTS: 15-50 Contact: Charlotta Polacek, chapo@vet.dtu.dk Place: DTU Vet, Bülowsvej 27, 1870 Frederiksberg C
Projects 14
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