Terence S. Dermody, MD
- Vira I. Heinz Professor and Chair, Department of Pediatrics
- Professor, Department of Microbiology and Molecular Genetics
- Member, Graduate Program in Microbiology and Immunology (PMI)
- Member, Integrative Systems Biology (ISB) Graduate Program
Education & Training
- MD, Columbia University, 1982
- BS in Biological Sciences, Cornell University, 1978
Research Interests
Our laboratory studies the pathogenesis of mammalian reovirus infection. Reovirus is an enteric, neurotropic virus that infects many mammalian species, including humans, but disease is restricted to the very young. Research in the Dermody laboratory encompasses several interrelated themes to better understand viral and cellular determinants of disease. These include viral attachment and entry into cells, genome replication and packaging, egress of viral progeny from infected cells, and functions of viral receptors in disease pathology. We also have established a link between reovirus and blockade of immunologic tolerance to new food antigens.
Projects in our laboratory are available to (i) identify and characterize reovirus receptors and entry strategies, (ii) discover mechanisms of reovirus replication factory formation and function, and (iii) elucidate pathways of reovirus dissemination and tropism in the host and interactions with innate and adaptive immune mediators. We employ genetic screens, biochemical assays, cell imaging, and organismal biology to advance our experimental goals. We collaborate extensively with structural biologists, biophysicists, cell biologists, and neuroscientists and enjoy working with interdisciplinary teams.
Publications
Bouziat, R., Hinterleitner, R., Brown, J. J., […], Dermody, T. S., and B. Jabri. Reovirus infection breaks tolerance to dietary antigens and promotes development of celiac disease. Science. 356:44-50, 2017. PMCID: PMC5506690
Fernández de Castro, I., Tenorio, R., Ortega-González, P., Knowlton, J. J., Zamora, P. F., Lee, C. H., Mainou, B. A., Fernández, J. J., Dermody, T. S., and C. Risco. A modified lysosomal organelle mediates non-lytic egress of reovirus. J. Cell Biol. 219:e201910131, 2020. PMCID: PMC7337502
Knowlton, J. J., Gestaut, D. R., Ma, B., Taylor, G. M., Seven, A. B., Leitner, A., Wilson, G. J., Shankar, S., Yates, N., Prasad, B. V. V., Aebersold, R., Chiu, W., Frydman, J., and T. S. Dermody. Structural and functional dissection of reovirus capsid folding and assembly by the prefoldin-TRiC/CCT chaperone network. Proc. Natl. Acad. Sci. USA. 118:e2018127118, 2021. PMCID: PMC7980406
Sutherland, D. M., Streßl, M., Koehler, M., Welsh, O. L., Yu, X., Hu, L., Dos Santos Natividade, R., Knowlton, J. J., Taylor, G. M., Moreno, R. A., Wörz, P., Lonergan, Z. R., Aravamudhan, P., Guzman-Cardozo, C., Kour, S., Pandey, U. B., Alsteens, D., Wang, Z., Prasad, B. V. V., Stehle, T., and T. S. Dermody. NgR1 binding to reovirus reveals an unusual bivalent interaction and a new viral attachment protein. Proc. Natl. Acad. Sci. USA. 120:e2219404120, 2023. PMCID: PMC10268256
Shang, P., Dos Santos Natividade, R., Taylor, G. M., Ray, A., Welsh, O. L., Fiske, K. L., Sutherland, D. M., Alsteens, D., and T. S. Dermody. NRP1 is a receptor for mammalian orthoreovirus engaged by distinct capsid subunits. Cell Host Microbe 32:980-995, 2024. PMCID: PMC11176008