Taraschi, Theodore F.
Theodore F. Taraschi, PhD
Jefferson Alumni Hall, Suite 209
Philadelphia, PA 19107
PhD, Rutgers University, Chemistry - 1980
Associate Dean for Research, Jefferson Medical College
Research and Clinical Interests
The invasion of erythrocytes by Plasmodium falciparum parasites produces aninfection that causes major changes in the structure, composition, antigenicity and function of the host cell membrane. During infection, the parasite actively imports obligate nutrients from the serum and exports lipids, proteins and membranes to the erythrocyte cytoplasm and the erythrocyte membrane. The regulation of these pathways must be underparasite control since mature erythrocytes have limited lipid synthetic or metabolic capabilities and do not have the machinery to synthesize or process proteins. Elucidation of trafficking pathways is complex in Plasmodia-infected erythrocytes compared to other eukaryotic cells, since the parasite is separated from the serum by its plasma membrane, the parasitophorous vacuolar membrane PVM and the erythrocyte membrane. There remains a long-felt need to identify the cellular components of these trafficking pathways to gain a better understanding of transport mechanisms in malaria-infected erythrocytes.
The laboratory is engaged in three areas of inquiry:
- Elucidation of parasite protein trafficking pathways from intracellular parasites to the erythrocyte cytosol and host cell membrane.
- Determination of the mechanism of hemoglobin uptake and transport by intraerythrocytic parasites
- Characterization of parasite DNA repair pathways (e.g. base excision and mismatch repair). Continued identification of the cellular components of these trafficking pathways to gain a better understanding of transport mechanisms in malaria-infected erythrocytes.
Most Recent Peer-Reviewed Publications
- Defining the morphology and mechanism of the hemoglobin transport pathway in Plasmodium falciparum-infected erythrocytes
- Malaria drug resistance is associated with defective DNA mismatch repair
- The longin domain regulates the steady-state dynamics of sec22 in plasmodium falciparum
- A new model for hemoglobin ingestion and transport by the human malaria parasite Plasmodium falciparum
- Expression and biochemical characterization of the Plasmodium falciparum DNA repair enzyme, flap endonuclease-1 (PfFEN-1)
- Expression and biochemical characterization of Plasmodium falciparum DNA ligase I
- Delivery of the malaria virulence protein PfEMP1 to the erythrocyte surface requires cholesterol-rich domains
- Effects of D-myo-inositol 1-phosphate on the transfer function of phosphatidylinositol transfer protein α
- L-α-Glycerylphosphorylcholine inhibits the transfer function of phosphatidylinositol transfer protein α
- Generation of an erythrocyte vesicle transport system by Plasmodium falciparum malaria parasites
- Evidence of an intraerythrocytic secretory pathway in erythrocytes infected with Plasmodium falciparum
- Vesicle-mediated trafficking of parasite proteins to the host cell cytosol and erythrocyte surface membrane in plasmodium falciparum infected erythrocytes
- Gelonin is an unusual DNA glycosylase that removes adenine from single-stranded DNA, normal base pairs mismatches
- Activity of phosphatidylinositol transfer protein is sensitive to ethanol and membrane curvature
- Evidence for vesicle-mediated trafficking of parasite proteins to the host cell cytosol and erythrocyte surface membrane in Plasmodium falciparum infected ertythrocytes
- DNA base excision repair in human malaria parasites is predominantly by a long-patch pathway
- Letter to the editor 
- Direct binding of lupus anticoagulant antibodies to nonbilayer phosphatidylethanolamine
- Characterization of class II apurinic/apyrimidinic endonuclease activities in the human malaria parasite, Plasmodium falciparum
- Phospholipid-bound β2-glycoprotein I induces the production of anti-phospholipid antibodies