Little is known about the HTLV-I enzyme, or protease, that cuts long strings of amino acids to form functional proteins that make a mature HTLV-I virus -- a distant cousin of the HIV virus that causes AIDS. About 250 researchers worldwide are studying the HTLV-I protease, and among them are researchers at the Georgia Institute of Technology. They will present their findings on April 1 at the 227th national meeting of the American Chemical Society (ACS) in Anaheim, Calif.
"There are currently no good ways to treat HTLV-I and prevent the spread of the virus," said Suzanne B. Shuker, an assistant professor of chemistry and biochemistry at Georgia Tech. "Therapies that inhibit the life cycle of the virus have potential as treatments for HTLV-I infection. The protease from HTLV-I is therefore an attractive target for inhibitor design."
Researchers in Shuker's laboratory have been studying this protease for five years, building on research begun at Georgia Tech 12 years ago by former Professor Rick Ikeda, now at the National Institutes of Health. As they test possible inhibitor compounds, Shuker and her students are also working to understand more about the enzyme's activity and structure to help in the development effort. A Georgia Tech and Centers for Disease Control (CDC) seed grant is funding the current work.
Research team member Bryan Herger, a fourth-year Ph.D. student in Shuker's lab, studies how the protease functions and how it identifies the amino acids it's supposed to cut. This information helps fourth-year Ph.D. student Kelly
Dennison and other team members find compounds that mimic the HTLV-I protease's process of cutting amino acid
Contact: Jane Sanders
Georgia Institute of Technology Research News