DAVID S. PETERSON
Associate Professor

The primary research focus of my laboratory is to understand the role of parasite adhesion proteins in the interaction of Plasmodium falciparum with receptors on host cells. The particular parasite proteins I am interested in are all members of the duffy binding-like (dbl) superfamily of adhesion proteins. Different members of this large family of related proteins have been demonstrated to play a central role in two critical events in the parasites life cycle; invasion of red blood cells and adherence of parasitized red blood cells to the vascular endothelium and to placental syncytiotrophoblasts. We are currently characterizing one putative erythrocyte binding protein, to determine its role in red cell invasion. Related work seeks to determine the degree of gene polymorphism and differences in gene expression in the erythrocyte binding protein family.

Peterson Lab Group

Recently we have also begun to test the expression of various Plasmodium proteins in a novel expression host, the free-living protozoan Tetrahymena thermophila. We have shown that proteins such as TRAP and the CSP can be expressed in Tetrahymena, and appear to be functional. We are now investigating the use of the Tetrahymena expression system for characterization of the erythrocyte binding protein family of Plasmodium falciparum.

Our lab is also part of a collaborative effort with the laboratory of Dr. Julie Moore in this department to study how the binding of parasitized erythrocytes to host cells effects host cell function, particularly as it relates to immune function.

RECENT PUBLICATIONS

Search PubMed for "peterson, ds"

Lucchi, N., Koopman, R., Peterson, D. S. and Moore, J. M. 2006. Plasmodium falciparum-Infected Red Blood Cells Selected For Binding To Cultured Syncytiotrophoblast Bind to Chondroitin Sulfate A And Induce Tyrosine Phosphorylation In the Syncytiotrophoblast. Placenta, 27(4-5):384-94.

Drummond, P. B. and Peterson, D. S. 2005. An analysis of genetic diversity within the ligand domains of the Plasmodium falciparum ebl-1 gene. Molecular and Biochemical Parasitology, 140(2):241-5.

Chaisavaneeyakorn, S., Lucchi, N., Abramowsky, C., Othoro, C., Chaiyaroj, S. C., Shi, Y. P., Nahlen, B. L., Peterson, D. S., Moore, J. M. and Udhayakumar, V. 2005. Immunohistological Characterization of Macrophage Migration Inhibitory Factor (MIF) Expression in Malaria-Infected Placenta. Infection and Immunity, 73(6):3287-93.

Peterson, D. S., Asokan, K. Gao,Y. and Gaertig, J. 2002. The Circumsporozoite protein of Plasmodium falciparum is expressed and localized to the cell surface in the ciliate Tetrahymena thermophila. Molecular and Biochemical Parasitology, 122:119-126.

Baig, S. Damian, R. T. and Peterson, D. S. 2002. A Novel Cathepsin B Active Site Motif is Shared by Helminth Bloodfeeders. Experimental Parasitology, 101(2-3):83-9, 2002.

Jaso-Friedman, L., Peterson, D. S., Gonzalez, D. S. and Evans, D. L. 2002. The antigen receptor (NCCRP-1) on catfish and zebrafish nonspecific cytotoxic cells belongs to a new gene family characterized by an F-box associated (FBA) domain. Journal of Molecular Evolution, 54(3): 386-395.

Peterson, D. S. 2001. Plasmodium gallinaceum: Cloning and characterization of dihydrofolate reductase-thymidylate synthase. Experimental Parasitology, 99(2):111-4.

Adams, J. H., Kaneko, O., Blair, P. L. and Peterson, D. S. 2001. An Expanding ebl Family of Plasmodium falciparum. Trends in Parasitology, 17:6:297-299.

Peterson, D. S. and Wellems, T. E. 2000. EBL-1, a putative erythrocyte binding protein of P. falciparum, maps within a favored linkage group in two genetic crosses. Molecular and Biochemical Parasitology, 105(1):105-13.

Email
dspete@uga.edu

Office
S345C Coverdell
706-542-5242

Degrees
BS, University of California, Davis, 1979
PhD, University of California, Irvine, 1988