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Virus-fighting protein could lead to better HIV treatment
Greenville, N.C. (May 25, 2010) — An East Carolina University scientist’s research involving a naturally occurring cellular protein could lead to better treatments for HIV as well as cancers and other viruses.
Colin Burns, an associate professor of chemistry, with help from graduate student Chris Wilson, narrowed down which part of that protein, prothymosin-alpha, contains the highest concentration of virus-fighting capabilities. That finding, in turn, has helped researchers at Duke University and the Mount Sinai School of Medicine learn how the protein can block viral replication once the human immunodeficiency virus invades cells.
“Some of the molecules that we’re developing will allow us to study HIV replication in a little more detail,” Burns said. “Then, once we have active molecules and we know what it’s interacting with in the cells, particularly, we have a target that we can use to design more active compounds that are even more effective or more potent.”
The scientists’ findings were published last week in the Proceedings of the National Academy of Sciences.
The findings may help researchers find more effective, more economical ways to combat the spread of the human immunodeficiency virus in infected people. Prothymosin-alpha appears to tell human cells to produce interferon, a substance that triggers the immune system to eradicate pathogens such as viruses.
An effective virus fighter, interferon is used in treating hepatitis. In combination with other therapies, interferon is also used to treat certain cancers. The injections are costly, however, Burns said; understanding prothymosin-alpha’s properties may help scientists design an antiviral medication that is more economical and, ultimately, more potent.
To gain understanding, Burns’ lab synthesized pieces of prothymosin-alpha and found the part of the protein molecule that has the ability to suppress HIV replication. “Proteins are usually rather large molecules,” Burns said. “Sometimes it’s only a part of it that is responsible for the majority of the biological activity. A lot of times you can make a small piece of the molecule, and that way you’ve reduced the complexity of the problem.”
Burns’ collaborators have identified a key molecule that prothymosin-alpha interacts with called Toll-like Receptor 4, he said. “We are planning to study how it and prothymosin-alpha fit together, as it is their interaction that ultimately leads to production of interferon,” Burns said. “With this knowledge, we may be able to design more potent molecules.”
The study was reported by Mary Klotman, chair of the department of medicine at Duke and the senior author of the paper; Mount Sinai assistant professors Arevik Mosoian and Avelino Teixeira; and colleagues Leif Sander, G. Luca Gusella, Cijiang He, Magarian Blander and Paul Klotman from Mount Sinai; as well as Burns.
Burns’ research was funded in part by a $25,000 N.C. Biotechnology Center grant.
Colin Burns, associate professor of chemistry
East Carolina University
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