Biochemists a step closer to battling TB :: Namibia Internet Gateway cc ::

Articles: Biochemists a step closer to battling TB

Posted by admin on Tuesday, May 11, 2004 - 07:00 AM

A study conducted by the biochemists from the University of Wisconsin-Madison, has opened the doors for developing a new family of antibiotics for treating diseases that still claim as many as 3 million lives annually worldwide.
The biochemists have discovered the working of an enzyme that plays a crucial role in causing infectious diseases like tuberculosis and leprosy. Laura L. Kiessling, an UW-Madison professor of chemistry and the lead author and her team have detailed the workings of a key enzyme that the bacterium requires maintaining the integrity of its cell walls. Enzymes are proteins that initiate chemical reactions within plant and animal cells. "We've figured out how this enzyme works. If you knock it out, the bacteria aren't viable. It's an essential enzyme," Kiessling was quoted by Nature, as saying. The family of bacteria that causes tuberculosis (TB) and leprosy are notoriously sturdy and most of the traditional antibiotics don't work against these bacterias. The TB microbe's success and resistance to traditional drugs is attributed in largely to its multilayered cell wall, composed of chicken wire-shaped molecules wrapped around an inner membrane. The enzyme is required for the TB bacterium to build its cell wall. The enzyme, in turn, depends on a derivative of vitamin B2 to make a cell wall building block. The research done by Kiessling's group shows that the enzyme uses the vitamin in a new way, which also gives it a new biological role. Detailing the interplay between vitamin B2 and the enzyme can provide a blueprint for inhibitors of the enzymes that keep the bacterium's cell walls intact and as a result, Kiessling's group has effectively identified a target for drug manufactures interested in developing new antibiotics to combat TB and other diseases such as leprosy, which are caused by similar types of bacteria. "Because we understand the mechanism better, we can design inhibitors of this enzyme," Kiessling explained.

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