Audrey Lamb

Associate Professor
Ph.D., Vanderbilt University, 1998
Post doctoral fellow, Northwestern University, 1998-2002
Primary office:
785-864-5075
5060 Haworth Hall

Structural and functional analysis of enzymes associated with iron uptake.

With the exception of a few microbial organisms, iron is required for life on earth.  Iron serves as an important cofactor for a variety of enzymes that perform crucial reactions, including roles in cellular respiration, nucleic acid synthesis, and resistance to reactive oxygen intermediates.  Fe(III) is very insoluble and frequently biologically inaccessible such that the concentration of available iron in the human host is ~10-9 mM.  Since a typical pathogenic bacterium requires ~1 mM iron for optimal growth, these organisms have developed elaborate systems to scavenge iron from the host.  The pathogens that we study use low molecular weight iron chelators called siderophores.  The bacteria synthesize, secrete, and then selectively take up the iron-loaded siderophore to colonize human tissues.  Non-ribosomal peptide synthetases (NRPSs) and their accessory proteins are a fascinating collection of enzymes required for the production of these bioactive peptides.  Siderophore biosynthetic enzymes are found in plants, fungi and bacteria, frequently having no human homologues, making them attractive targets for the development of new antimicrobial compounds.  The goal of the lab is to understand the structure-function relationships that drive the biosynthesis of siderophores, compounds linked to virulence and pathogenesis in a variety of deadly bacteria.  The ultimate outcome of the work will be the structural biology and mechanistic enzymology required for the development of new antibiotics to fight many bacterial infections, including P. aeruginosa, an opportunistic pathogen that is problematic for cystic fibrosis and other susceptible patients, as well as for bacteria that generate chemically-related siderophores such as Yersinia pestis (plague), Vibrio cholera (cholera) and Mycobacterium tuberculosis (tuberculosis).  The enzymes we study are also of interest to the protein engineering community, as many bioactive peptides contain similar chemical moieties and homologous enzymes are found in biosynthetic pathways of a variety of natural products.  Two examples are epothilone and cyclosporin.  Therefore, our work may also impact the design of new anti-cancer and immunosuppressive therapeutics.

 

Representative Publications

 

Search PubMed for articles by Audrey L. Lamb.


Home to 50+ departments, centers, and programs, the School of the Arts, and the School of Public Affairs and Administration
KU offers courses in 40 languages
No. 1 ranking in city management and urban policy —U.S. News and World Report
One of 34 U.S. public institutions in the prestigious Association of American Universities
26 prestigious Rhodes Scholars — more than all other Kansas colleges combined
Nearly $290 million in financial aid annually
46 nationally ranked graduate programs.
—U.S. News & World Report
Top 50 nationwide for size of library collection.
—ALA
23rd nationwide for service to veterans —"Best for Vets," Military Times
Susan Egan (professor and chair) and Dave Benson (chemistry) are the recipients of a three year Beckman Scholars Program Grant, which has the goal of stimulating, encouraging and supporting research activities by exceptionally talented, full-time undergraduate students pursuing research activities in chemistry, biochemistry, biology and the medical sciences. The KU program has 15 mentors from Molecular Biosciences and Chemistry, and will support two undergrad students per year. The students will receive a stipend totaling $22,000 to support their research (for two academic years and two summers), travel funds to present their research at a conference in their field, and the lab of their mentor will receive $5,000 for supplies to support their research.
Susan M. Egan | Department of Molecular Biosciences
Google Scholar Profile Susan M. Egan ProfessorChair, Department of Molecular Biosciences sme@ku.edu Primary office: (785) 864-4294 8031 Haworth (Lab office) Second office: (785) 864-4294 2040 Haworth (Chair's office) Regulation of bacterial transcription, Development of novel anti-bacterial agents.…