0806OSUresearcherawardedko.cfm OSU researcher awarded $1.34 million grant to continue work
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OSU researcher awarded $1.34 million grant to continue work

Oklahoma

Approximately nine months ago, researchers in the Division of Agricultural Sciences and Natural Resources at Oklahoma State University made a significant discovery with major implications in the medical field.

A structural biochemist in the department of biochemistry and molecular biology, Junpeng Deng, along with his first-year Ph.D. student Brian Krumm, solved a three-dimensional crystal structure of a poxvirus protein in the act of disarming a human immune molecule, interleukin-18 (IL-18).

This scientific breakthrough was the first step toward a pharmaceutical medication for poxvirus-caused diseases, aid in national and international security efforts and a treatment for autoimmune diseases.

At that time, Deng said, "This is just the beginning." Turns out, he was right. Deng was recently awarded a four-year $1.34 million grant from the National Institutes of Heath to continue this research.

"Obtaining federal funding is a highly competitive process that involves intensive peer review and evaluation by experts throughout the scientific community," said Gary Thompson, biochemistry and molecular biology department head. "A grant of this magnitude awarded by the National Institutes of Health reflects both the importance of this research and the quality of the OSU team conducting the research."

While solving the three-dimensional structure last December was the first hurdle, it only tells part of the story. That research allowed the understanding of where the poxvirus attaches to the IL-18, but Deng is now looking at how the IL-18 is functioning.

In a nutshell, the IL-18 must bind with its two receptor proteins on the cell membrane to activate the human immune response. Deng's proposal to the NIH was to study the mechanism of how the signal to activate the immune response is occurring and is regulated.

"No one really knows how the interleukin-18 activates its receptors," said Deng. "Once we know where it binds and how it activates, the story will then be more complete."

With this information, Deng, Krumm and their collaborators from the Texas Health Science Center in San Antonio will be able to develop a protein drug to bind those receptors to regulate the immune system activities.

Deng is hopeful that this research will provide scientific knowledge, and be applicable to practical issues regarding human health and security.

"This contribution is significant because it will fill the gap of our current knowledge on interleukin-18's activation pathway, and will provide important clues on how to modulate IL-18 activity," he said. "It may benefit efforts in developing treatments against some autoimmune and inflammatory diseases, in developing immunotherapies against other infectious diseases and cancer and in combating bioterrorism."



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