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Disrupting Protein “Factories” Could Lead to Treatments for HIV, Cancer

MU researcher selected as PEW Scholar; Will receive $240,000 to support research

June 14th, 2012

Story Contact: Christian Basi, 573-882-4430, BasiC@missouri.edu

COLUMBIA, Mo. — Inside the body, the ribosome is known as the protein “factory.” This large molecule creates proteins, which are responsible for many biological functions. When bacteria or a virus, such as HIV, invades the body, it disrupts the functions of the ribosome, eventually creating havoc with some biological functions. Now, a University of Missouri researcher has been nationally recognized for his work to stop this disruption and possibly create a treatment for HIV and other diseases, such as cancer.

“The ribosome moves along a chain of messenger RNA molecules in a particular pattern, typically three molecules at a time, as it gathers information from the RNA and determines which proteins it should create,” said Peter Cornish, a professor of biochemistry in the MU School of Medicine. “Sometimes, when certain viruses enter the body, this movement is disrupted and ‘frame-shifting’ occurs. So instead of reading the RNA molecules three at a time, a frame-shifted ribosome might make a temporary shift by a single molecule. Now, it’s still reading RNA molecules three at a time, but it’s getting the information in a different order and creating different proteins that are required for viral replication and propagation.”

Through his research, Cornish is determining how to get the ribosome’s process back on track, while simultaneously destroying or containing the virus or bacteria. Currently, he has two potential solutions to this problem. The first solution is to stop the frame-shifting from happening. For example, if a drug could be administered to get the ribosome back on track, the proteins needed for viral replication would not be produced.

The other method is to shut down or stall the ribosome factory. For example, in one E. coli cell, more than 15,000 ribosomes might be present. If the ribosomes in the E. coli cell were shut down and unable to produce additional proteins, the bacteria would not be able to replicate. The body would eventually get rid of the foreign trespasser safely.

“Our bodies’ natural defenses are constantly working to keep us healthy,” Cornish said. “We only get sick when the viruses or bacteria are able to replicate enough to overwhelm our defenses. If we can determine how to stop them from replicating, the body’s defenses can take over and get rid of the invaders naturally.”

Cornish’s research also could be applied to cancer eventually. Cancer survives by replicating cells at a much faster rate than other areas of the body. As the cancer cells grow faster, they need more proteins. If a drug could be designed to stall the ribosome from producing proteins, the cancer would no longer have enough proteins to continue replicating.

Cornish believes that because the ribosome is such a large molecule, it might be possible to create a drug that would help the ribosome if it was disrupted and frame-shifting was occurring. However, scientists need to understand the fundamental biology of the ribosome and the communication links among molecules before drug development can begin.

While this research is at the molecular level, Cornish has drawn the attention of his peers at a much higher level, as he has been recognized as a 2012 Pew Scholar in Biomedical Sciences. This award recognizes him as one of the 22 most promising, young investigators in the field.

The awards are given to 22 scientists around the country and come with a $240,000 prize that is awarded over four years. Universities are only allowed one nomination for each campus. The only restriction on the money is that it should be used for furthering the scientist’s current research program. For more information about the Pew Scholar program, please visit: http://www.pewtrusts.org/our_work_category.aspx?id=194.

Cornish received his doctorate from Texas A&M University in 2005 and was in a post-doctoral program at the University of Illinois before coming to MU in 2010 for his current position. His research on this work has been published recently in the Proceedings of the National Academies of Science, Science, Molecular Cell and the Journal of Molecular Biology.

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