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SCIENCE MANAGEMENT TEAM

Dr. Scott Napper, Ph.D.
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Responsibilities:
♦ Program Manager: Emerging Diseases and Bacterial Virulence
Project Leader: BSE Vaccine Development and Prion Research; Johne's Disease; Molecular Pathogen Recognition
♦ Member: Science Management
♦ Member: Pathogenomics Research Program
♦ Member: Neonatal Immunization Program
♦ Associate Member: Department of Biochemistry, University of Saskatchewan

Education:
University of Saskatchewan, Department of Biochemistry, Ph.D. 1999


The Napper Lab (2007). Dr. Napper, centre, with lab mascot Ed the E. coli. From left to right, Peter Hedlin, Jean Potter, Jason Tomporowski, Gordon Crockford, Shakiba Jalal, Jyotsana Gupta, Ryan Arsenault, Jason Kindrachuk.

Current Research Interests:
1) Prion diseases in a variety of mammalian species are characterized by the conversion of the normal host protein (PrPC) to an abnormal infectious form (PrPSc). A research team led by Dr. Neil Cashman has identified and characterized a surface-exposed antibody-binding site which is present on PrPSc but not PrPC. This site is conserved among PrPSc of a wide variety of mammalian species, thus making it an excellent universal vaccine target for prevention and therapy of diseases such as BSE and CWD. The primary objective of this proposal is to develop vaccine formulations and vaccination protocols for ruminants which generate sustained levels of antibodies that react specifically with PrPSc but not PrPC.

2) Host-Pathogen Sensory Systems I am interested in the systems utilized by hosts and pathogens to detect and respond to each other. From the host perspective, my group is focusing on Toll-like Receptor 9. Currently, we are characterizing the interaction of this receptor with its nucleic acids ligands. On the bacterial side, we are studying the PhoPQ two-component system. Specifically, we are interested in characterizing the ability of this bacterial system to employ host defense molecules as triggers for the initiation of virulence. Our goal is to develop strategies that permit optimization of antimicrobial peptides to minimize the extent of bacterial response and therefore the likelihood of developing resistance.

3) Kinome Analysis Many host responses to a stimulus are regulated through reversible patterns of phosphorylation mediated by kinase enzymes. Our group is investigating methodologies for global, high-throughput analysis of host cell kinase activity, the kinome. This analysis is designed to complement the extensive gene expression analyses being conducted at VIDO.

Major Accomplishments:
establishment of a novel system to screen interactions of Toll-like Receptor 9 with nucleic acids
establishment of a system for optimization of host-defense peptides to minimize activation of bacterial defensive responses

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