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Researchers step closer to treatment of virulent hospital infection
Date:3/18/2011

and disrupting cell functions such as adhesion. The new research shows that what's known as single-domain antibodies bind to the C. difficile toxins with high affinity and interfere with the toxins' ability to damage cells.

"Llamas have normal antibodies like our own, but they have also developed a second type of antibody with a simpler structure. It is this simpler structure that allows us to make modifications and perform many detailed studies that are not easily done with other types of antibodies," says Ng. "The unique characteristics of these single-domain antibodies provide an attractive approach for developing new treatments for C. difficile."

These single-domain antibodies were discovered in 1993 in camelids, which include llamas and camels. Camelids produce conventional antibodies found in all mammals as well as heavy-chain antibodies from which single-domain antibodies are derived. These single-chain antibodies are 10 times smaller than those found in humans and can be more readily engineered into a drug.

Dr. Jamshid Tanha, the corresponding author of the study from the National Research Council in Ottawa says that understanding how camelid antibodies work will ultimately allow researchers to develop a new treatment for this important disease and potentially others.

"We are currently working with Dr. Ng's group to determine why these antibodies are successful," says Tanha.

Currently, licensing opportunities with biotechnology firms are being explored.


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Contact: Leanne Yohemas
leanne.yohemas@ucalgary.ca
403-540-6552
University of Calgary
Source:Eurekalert  

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