Professor of Microbiology
Phone:(206) 543-2820, (206) 685-2247
Office Location: Health Sciences, J-257A
Campus Box: 357735
Dr. Moseley obtained a B.A. in biology from the University of Dallas, an M.S. in microbiology from the Catholic University of America in Washington, D.C., and his Ph.D. in microbiology from the University of Washington, where he worked on the genetics of E. coli enterotoxins with Dr. Stanley Falkow. His postdoctoral training was at Stanford University. Dr. Moseley has worked as a microbiologist at the Walter Reed Army Institute of Research in Washington, D.C. and at the National Animal Disease Center in Ames, Iowa.
The major emphasis of the laboratory is the study of fimbrial adhesins of E. coli associated with human disease. The laboratory focuses on a family of E. coli fimbriae, the Dr adhesins, which can simultaneously bind to multiple receptors on human cells and tissues. These receptors include complement regulatory proteins, cell adhesion molecules, and collagen. We are interested in the nature of adhesin-receptor interactions, and how those interactions trigger cellular responses contributing to disease. Our investigations combine genetic, evolutionary, biochemical, and structural approaches to these questions.
Rashid, R.A., Tabata, T.A., Oatley, M.J., Besser, T.E., Tarr, P.I., Moseley, S.L. 2006. Expression of putative virulence factors of Escherichia coli O157:H7 differs in bovine and human infections. Infect. Immun. 74:4142-8.
Korotkova, N., Le Trong, I., Samudrala, R., Korotkov, K., Van Loy, C.P., Bui, A.L., Moseley, S.L., Stenkamp, R.E. 2006. Crystal structure and mutational analysis of the DaaE adhesin of Escherichia coli. J. Biol. Chem. 281:22367-77.
Korotkova, N., Cota, E., Lebedin, Y., Monpouet, S., Guignot, J., Servin, A.L., Matthews, S., Moseley, S.L. 2006. A subfamily of Dr adhesins of Escherichia coli bind independently to decay-accelerating factor and the N-domain of carcinoembryonic antigen. J. Biol. Chem. 281:29120-30.
Rashid, R.A., Tarr, P.I., Moseley, S.L. 2006. Expression of the Escherichia coli IrgA homolog adhesin is regulated by the ferric uptake regulation protein. Microb. Pathog. 41:207-217.
Korotkova, N., Chattopadhyay, S., Tabata, T.A., Beskhlebnaya, V., Vigdorovich, V., Kaiser, B.K., Strong, R.K., Dykhuizen, D.E., Sokurenko, E.V., Moseley, S.L. 2007. Selection for functional diversity drives accumulation of point mutations in Dr adhesins of Escherichia coli. Mol. Microbiol. 64:180-94.
Korotkova, N., Y. Yang, I. Le Trong, E. Cota, B. Demeler, J. Marchant, W. E. Thomas, R. E. Stenkamp, S. L. Moseley*, and S. Matthews*. 2008. Binding of Dr adhesins of Escherichia coli to carcinoembryonic antigen triggers receptor dissociation. Mol Microbiol 67:420-434. *Co-corresponding authors.
Korotkova N., Yarova-Yarovaya, Y., Tchesnokova V., Yazvenko, N., Carl, M.A., Stapleton, A.E. and Moseley, S.L. 2008. E. coli DraE adhesin – associated bacterial internalization by epithelial cells is independently promoted by decay accelerating factor and CEACAM binding, and does not require the DraD "invasin". Infect. Immun. 76:3869-80.