News Release

Researchers open new line of attack on tuberculosis

Findings could show how to breach the bacterium's tough cell wall

Peer-Reviewed Publication

U.S. National Science Foundation

ARLINGTON, Va.-Chemists and biochemists at the University of Wisconsin-Madison, supported in part by the National Science Foundation (NSF), have discovered a new chink in the armor of the bacterial family that causes diseases such as tuberculosis and leprosy.

The researchers' findings, which are reported today (May 9) in the online edition of the journal Nature Structural & Molecular Biology, could lead to the development of a new family of antibiotics to treat those afflictions, which claim up to 3 million lives around the world every year. This prospect is especially welcome given the rapid spread of tuberculosis strains that are resistant to existing drugs.

Microbes that cause tuberculosis and leprosy, and related bacteria, are particularly tough adversaries because of their unique, multilayered cell walls, which render them virtually invulnerable to easy treatment. In the research reported today, however, UW chemist Laura L. Kiessling and her team have detailed the workings of a key enzyme the bacteria use to maintain the integrity of their cell walls. Enzymes are proteins that initiate chemical reactions within bacteria, plant and animal cells.

"We've figured out how this enzyme works," says Kiessling. "If you knock it out, the bacteria aren't viable."

Kiessling cautions that it takes years and many millions of dollars to develop a new drug. Nonetheless, this discovery opens up a whole new line of attack against TB and leprosy. "Because we understand the mechanism better, we can design inhibitors specific to this enzyme."

In the paper, Kiessling acknowledges support from an NSF Young Investigator award. "It is gratifying to see that seminal funding from NSF has helped Dr. Kiessling develop into a leading organic chemist," says NSF program officer, George Rubottom. "Her research, which covers the spectrum from synthesis to enzyme mechanism, highlights the unique role chemistry can play in solving extremely important biological problems."

###

A more detailed press release about this work will be available after the embargo lifts on the University of Wisconsin-Madison web site: http://www.news.wisc.edu/.

NSF Media Contact: M. Mitchell Waldrop, (703) 292-7752, mwaldrop@nsf.gov

UW-Madison Media Contact: Terry Devitt, (608) 262-8282, trdevitt@wisc.edu

NSF Program Officer: George Rubottom, (703) 292-4965, grubotto@nsf.gov

Principal Investigator: Laura L. Kiessling, (608) 262-0541, kiessling@chem.wisc.edu

The National Science Foundation is an independent federal agency that supports fundamental research and education across all fields of science and engineering, with an annual budget of nearly $5.58 billion. National Science Foundation funds reach all 50 states through grants to nearly 2,000 universities and institutions. Each year, NSF receives about 40,000 competitive requests for funding, and makes about 11,000 new funding awards. The National Science Foundation also awards over $200 million in professional and service contracts yearly.

Receive official National Science Foundation news electronically through the e-mail delivery system, NSFnews. To subscribe, send an e-mail message to joinnsfnews@lists.nsf.gov. In the body of the message, type "subscribe nsfnews" and then type your name. (Ex.: "subscribe nsfnews John Smith")

Useful National Science Foundation Web Sites:
NSF Home Page: http://www.nsf.gov
News Highlights: http://www.nsf.gov/od/lpa
Newsroom: http://www.nsf.gov/od/lpa/news/media/start.htm
Science Statistics: http://www.nsf.gov/sbe/srs/stats.htm
Awards Searches: http://www.fastlane.nsf.gov/a6/A6Start.htm


Disclaimer: AAAS and EurekAlert! are not responsible for the accuracy of news releases posted to EurekAlert! by contributing institutions or for the use of any information through the EurekAlert system.