Katrina Forest
Email:
forest@bact.wisc.eduAssociate Professor
Degrees
B.S., 1987, MIT
Ph.D., 1993, Princeton University
Postdoctoral Research
The Scripps Research Institute
Research Focus
With the advent of antibiotics in the 1940's, many of the threats and fears of bacterial disease were temporarily overcome. Today antibiotic resistance and newly emerging microbial diseases are among the greatest threats to human health. We study the structural aspects of microbial disease, using x-ray crystallography and complementary techniques. Our focus is the structure and assembly of Type IV pili, surface organelles that mediate attachment of pathogenic bacteria to eukaryotic cells. Pili are also required for twitching motility, which allows them to slither over and colonize eukaryotic host cells. We have recently solved the crystal structure of the pilus retraction protein PilT, a conserved nucleotide-binding protein essential for twitching motility. (The PilT hexamer is shown above, right.) Eventually, our understanding of the structure, assembly and antigenicity of pili and the mechanism of their assembly may lead to vaccines against many bacteria with Type IV pili.(The coordinates for pilin, phytochrome and other amazing proteins are available at the Protein Data Bank.)
Recent Publications:
- Satyshur, KA, Worzalla, GA, Meyer, LS, Heiniger, EK, Aukema, KG, Misic, AM and Forest, KT. Crystal Structures of the Pilus Retraction Motor PilT Suggest Large Domain Movements and Subunit Cooperation Drive Motility, Structure, 2007, in press.
- Wagner, JR, Brunzelle, JS, Forest, KT*, Vierstra, RD A light-sensing knot revealed by the structure of the chromophore-binding domain of phytochrome. Nature 438: 325-331, 2005.
- Aukema, KG, Kron, E., Herdendorf, TJ and Forest, KT. Functional dissection of a conserved motif within the pilus retraction protein PilT. J. Bact. 187: 611-618, 2005.
- Forest KT, Satyshur KA, Worzalla GA, Hansen JK and Herdendorf TJ. The pilus-retraction protein PilT: ultrastructure of the biological assembly. Acta Cryst D60:978-982, 2004.
- Craig L, Taylor RK, Pique ME, Adair BD, Arvai AS, Singh M, Lloyd SJ, Shin DS, Getzoff ED, Yeager M, Forest KT, Tainer JA. Type IV pilin structure and assembly: X-ray and EM analyses of Vibrio cholera Toxin-coregulated pilus and Pseudomonas aeruginosa PAK pilin. Mol. Cell 11:1139-1150, 2003.
- Herdendorf TJ and Forest KT. Aquifex aeolicus PilT, Homologue of a Surface Motility Protein, is a Thermostable Oligomeric NTPase. J. Bact. 184:5465-6471, 2002.
- Merz AJ and Forest KT. Bacterial Surface Motility: Slime Trails, Grappling Hooks and Nozzles. Current Biology. 12(8):R297-R303, 2002.
CLASSES
Microbiology at Atomic Resolution
