Suzanne Walker

Professor of Microbiology and Molecular Genetics Co-Director, Chemical Biology PhD Program

Department of Microbiology & Immunology
HIMI 1013
4 Blackfan Circle
Boston, MA 02115
Tel: 617-432-5488
Email: suzanne_walker@hms.harvard.edu

Website:
http://www.chem.harvard.edu/groups/walker/index.html
Lab Size: Greater than 10

Summary
The Walker Group has expertise in studying bacterial cell wall biosynthesis and its inhibition.  We have developed chemical approaches to study the membrane-linked steps of peptidoglycan and teichoic acid biosynthesis, and have made fundamental contributions to understanding the enzymes involved in these processes and the mechanisms of action of antibiotics that inhibit them.  We work on Gram positive organisms, including the pathogens Staphylococcus aureus and Enterococcus faecalis, and a major research focus includes exploring novel strategies to overcome antibiotic resistant microorganisms.  My research program combines organic chemistry, enzymology, high throughput screening, biophysics, and bacterial genetics to address problems of interest. 

Publications

Ortiz-Meoz RF, Merbl Y, Kirschner MW, Walker S. Microarray discovery of new OGT substrates: The medulloblastoma oncogene OTX2 is O-GlcNAcylated. J. Am. Chem. Soc. 2014; 136:4845-8.

Lazarus MB, Jiang J, Kapuria V, Bhuiyan T, Janetzko J, Zandberg WF, Vocadlo DJ, Herr W, Walker S. HCF-1 is cleaved in the active site of O-GlcNAc transferase. Science 2013; 342:1235-9.

Lazarus MB, Jiang J, Gloster TM, Zandberg WF, Whitworth GE, Vocadlo DJ, Walker S.  Structural snapshots of the reaction coordinate for O-GlcNAc transferase.  Nat Chem Biol 2012; 8:966-8.

Brown S, Xia G, Luhachack LG, Campbell J, Meredith TC, Chen C, Winstel V, Gekeler C, Irazoqui JE, Peschel A, Walker S.  Methicillin resistance in Staphylococcus aureus requires glycosylated wall teichoic acids. Proc Natl Acad Sci USA 2012; 109:18909-14.

Jiang J, Lazarus M, Pasquina L, Sliz P, Walker S. A neutral diphosphate mimic that crosslinks the active site of human O-GlcNAc transferase. Nat Chem Biol 2012; 8:72-7.