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Karen Ottemann
Associate Professor of Environmental Toxicology
• B.S, University of California, Davis (Bacteriology)
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Ph.D., Harvard University (Microbiology and Molecular Genetics)
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Postdoctoral Fellow, University of California, Berkeley (Biochemistry)
Office: 454 PSB,
Office Hours:
Email: ottemann@etox.ucsc.edu
Phone: (831) 459-3482
Lab Phone: (831) 459-4780
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Research
Group: Ottemann
Lab | UCSC
Biomedical Research | Ottemann
Lab Biomedical Research
How pathogenic bacteria such as Helicobacter pylori use environmental
cues to establish infection.
How pathogenic bacteria such as Helicobacter pylori use environmental
cues to establish infection.
 For pathogenic bacteria to set up an infection, they
must know that they have arrived at the proper location. Karen Ottemann's
laboratory investigates how bacteria translate chemical and physical
cues in their host environment into a response that allows them to
colonize a mammalian host.
Ottemann lab members are particularly interested in
how pathogens use swimming during infection, using the bacterium
Helicobacter pylori as a model for this ability. This pathogen infects
some 3 billion people and can lead to serious disease, including
ulcers and cancer. Bacteria do not swim at random, but instead direct
their motility (chemotaxis) by the activity of sensing proteins called
chemoreceptors. The chemotaxis system thus allows us to examine the
types of cues sensed by mammalian pathogens. We recently discovered
two of the first chemoreceptors known to aid in the process of bacterial
colonization.
H. pylori establishes infection by moving from its
host's stomach lumen to the mucous layer, where it can live for decades.
Evidence suggests that bacteria have sophisticated molecular machinery
for sensing the chemical environment of their host and use this information
to relocate to specific sites in their host where they have the best
chance for their own survival. To date, scientists have only been
able to identify a few of the host conditions to which microbes respond.
Enumerating such factors will not only provide insights into the
basic science of bacteriology, but may also help scientists identify
new antibiotic targets to combat destructive pathogens.
Selected
Publications
K. Terry, A. C. Go, K. M. Ottemann. 2006. Proteomic mapping of a suppressor of non-chemotactic cheW mutants reveals that Helicobacer pylori contains a new chemotaxis protein. Molecular Microbiology 61:871. http://www.blackwell-synergy.com/doi/abs/10.1111/j.1365-2958.2006.05283.x
D J. McGee, M L. Langford, E L. Watson, J E. Carter, Y T. Chen, and K M. Ottemann. 2005. Colonization and inflammation deficiencies in Mongolian gerbils infected by Helicobacter pylori chemotaxis mutants. Infection and Immunity. 73 (3), pp. 1820-1827. Postprint available: http://repositories.cdlib.org/postprints/707
K Terry, S M. Williams, L Connolly, and K M. Ottemann. 2005. Chemotaxis plays multiple roles during Helicobacter pylori animal infection. Infection and Immunity. 73 (2), pp. 803-811. Postprint available: http://repositories.cdlib.org/postprints/706
Andermann, T. M., Y.-T. Chen, and K. M. Ottemann.
2002. Two predicted chemoreceptors promote Helicobacter pylori infection. Infection and Immunity 70:5877-5881. View this publication.
Ottemann, K. M. and A. Lowenthal. 2002 Helicobacter
pylori uses Motility for Initial Colonization and to Attain Robust
Infection.
Infection and Immunity 70:1984-1990. View this publication.
Ottemann, K. M.*, W. Xiao*, Y.-K. Shin, and D. E.
Koshland, Jr. 1999. A Piston Model for Transmembrane Signaling
of the Aspartate
Receptor. Science 285:1751-1754. View
*These authors contributed equally to this work.
(Commentary by Gerstein and Chothia, Science 285:16982).
Ottemann, K. M., T. E. Thorgeirsson, A. F. Kolodziej,
Y.-K. Shin and D. E. Koshland, Jr. 1998. Direct Measurement of
Small
Ligand-Induced
Conformational Changes in the Aspartate Chemoreceptor using
EPR. Biochemistry 37:7062-7069.
Ottemann, K. M. and D. E. Koshland, Jr. 1997. Converting
a transmembrane receptor to a soluble receptor: Recognition
domain
to effector
domain signaling after excision of the transmembrane domain.
Proc. Natl. Acad. Sci. USA 94:11201-11204.
Ottemann, K. M. and J. F. Miller. 1997. Roles for
motility in bacterial-host interactions. Molecular Microbiology
24:1109-1117.
Ottemann, K. M. and J. J. Mekalanos. 1996. The ToxR
protein of V. cholerae forms homodimers and heterodimers. J.
Bacteriology 178:156-162.
Ottemann, K. M., and J. J. Mekalanos. 1995. Analysis
of Vibrio cholerae ToxR function by construction
of novel fusion proteins.
Molecular Microbiology. 15:719-731.
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