The host innate immune system plays an essential role in detecting invading viruses and in initiating and orchestrating antiviral responses. In order to establish productive infections, viruses have to effectively inhibit this host response. This leads to an evolutionary arms race between the host and the virus.
Our research focuses on the interaction between viruses with the immune system of their hosts. We are studying how viral nucleic acids are detected in vertebrates, which antiviral pathways are activated and how viral molecules interfere with these processes.
Major research objectives are the elucidation of the molecular mechanisms that determine virus host range and virulence. Viruses that are studied in our laboratory include Poxviruses, Influenza viruses, Herpesviruses, Iridoviruses, Ebola virus and Tumor viruses.
Rothenburg, S., Chinchar V.G. and Dever, T.E. 2011. Characterization of a Ranavirus Inhibitor of the Antiviral Protein Kinase PKR. BMC Microbiology, 11:56.
Rothenburg, S., Seo, E., Gibbs, J.S., Dever, T.E. and Dittmar, K. 2009. Rapid evolution of protein kinase PKR alters sensitivity to viral inhibitors. Nature Structural & Molecular Biology, 16, 63-70
Rothenburg, S., Deigendesch, N., Dey, M., Dever, T.E. and Tazi, L. 2008. Double-stranded RNA activated protein kinase PKR of fishes and amphibians: varying number of double-stranded RNA binding domains and lineage specific duplications. BMC Biology, 6:12
Deigendesch, N. Koch-Nolte, F. and Rothenburg, S. 2006. ZBP1 subcellular localization and association with stress granules is controlled by its Z-DNA binding domains. Nucleic Acids Research, 34: 5007-5020
Rothenburg, S., Deigendesch N., Dittmar, K, Koch-Nolte, F., Haag, F., Lowenhaupt, K. and Rich, A. 2005. A PKR-like eukaryotic initiation factor 2α kinase from zebrafish contains Z-DNA binding domains instead of double-stranded RNA binding domains. Proceedings of the National Academy of Sciences of the United States of America, 102:1602-1607.