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FRISC: The Faculty Research Interests Science Comparator |
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Assistant Professor of Internal Medicine and Microbiology
Molecular Microbiology
Office:
(214) 648-3625
FAX: (214) 648-9478
Email: simon.daefler@email.swmed.edu
Fluorescence-based isolation of bacterial genes expressed within host cells.
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Score: 0.436 |
Our laboratory is interested in the mechanism of how Gram
negative bacteria employ complex machineries to force-feed macromolecules into their
eukaryotic host cell and how this then determines the interaction between bacterium and
host. Our model system is Salmonella typhimurium . S.typhimurium uses two
type III secretion systems that are encoded by two independent chromosomal pathogenicity
islands (Salmonella pathogenicity island 1 and 2: SPI 1 and SPI 2) to target proteins
across its two lipid membranes and peptidoglycan layer into the host cytosol. Targeted SPI
1 substrates trigger signaling processes in the host cell that lead to the uptake of
Salmonella in an endosomal compartment. Targeted SPI 2 proteins negotiate the
intracellular fate of Salmonella within the host cell.
The current model envisions that components of the type III
systems assemble into a protein conduit in a stepwise fashion. Such a complex has to span
bacterial inner and outer membrane and the eukaryotic host cell or endosomal membrane. The
translocation of the substrates can be divided into two steps: translocation of substrates
across the bacterial envelope and delivery into the eukaryotic cytosol. Our goal is to
characterize this pathway at the molecular level.
Secreted bacterial effector molecules are likely to interact
with specific targets in the eukaryotic host cell. Our goal is to identify those targets
and determine the role this interaction plays in the intracellular trafficking of the
bacterium.
Selected Publications:
Daefler, S. (1999) Type III secretion by Salmonella typhimurium does not
require contact with a eukaryotic host, Mol. Microbiol . 31:45-51
Daefler, S., Russel, M. (1998) The Salmonella typhimurium InvH protein is an
outer membrane lipoprotein required for the proper localization of InvG. Mol.
Microbiol. 28:1367-1380
Daefler, S., Guilvout, I., Hardie, K.R., Pugsley, A.P., Russel, M. (1997) The
carboxy-terminal domain of the secretin PulD contains the binding site for PulS and
confers dependence on PulS for pIVf1 function. Mol. Microbiol. 24:465-475
Daefler, S., Russel, M., Model, P. (1997) Module swaps between related translocator
proteins pIVf1, pIVIKe, and PulD: Identification of a specificity domain. J. Mol.
Biol. 266:978-992
Page maintained by Stephanie
Robertson
Last updated: 17 Nov 2000
Extraction Method: Expand using Medical Synonyms-
Eliminated words list: MedlinePlus List
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Similarity Method: Weighted keyword count
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Database: Medline abstracts (1967 - Present)
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Publication Type: All
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Score Calculation Method: Cosine Similarity Method
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Results computed on: 6/9/2006