Kristen M. Ogden, Ph.D.
More Information
Innate immune responses to bacterial pathogens in the lung
Kristen earned her B.S. in Microbiology from Auburn University and her Ph.D. in Microbiology and Immunology from Vanderbilt University.
Research Information
RNA viruses are ubiquitous intracellular parasites that cause a number of important diseases. In order to successfully replicate in the different tissues and hosts they encounter, viruses must be able to efficiently bind, enter, and replicate in target cells and to adapt rapidly to environmental pressures. Several features, including large population size, fast replication rate, and short generation time, permit populations of RNA viruses to evolve much more rapidly than DNA-based organisms. These features also enable us to study viral evolution in real time. Research in the Ogden lab is focused on the tropism and diversity of segmented, double stranded RNA viruses of the Reoviridae family, including rotavirus and mammalian orthoreovirus (reovirus).
Rotavirus is an important cause of diarrheal disease that results in the deaths of hundreds of thousands of infants and young children worldwide each year. Licensed vaccines have significantly reduced the burden of rotavirus disease in several countries, but they may be exerting pressures leading to shifts in the antigenic makeup of predominantly circulating strains. Currently, our lab is interested in exploring the evolution of rotavirus in the post-vaccine era and identifying determinants of species and cell-type specificity for rotavirus, which may be dictated at the level of cell entry.
Our laboratory uses reovirus as an experimental system to study virus structure, virus-cell interactions, and viral diversity. A plasmid-based reverse genetics system permits the engineering of specific changes in the segmented reovirus genome to address questions of interest. Two main themes currently being explored in our laboratory are (i) diversity acquisition mechanisms for reovirus, including functions of the viral RNA polymerase and the frequency and dynamics of reassortment, and (ii) structure-function relationships of the reovirus attachment protein and cellular receptors.