CLEVELAND--Case Western Reserve University chemist Mary Barkley wants to find out what makes two pieces of a protein in the AIDS virus begin the biochemical processes that lead to AIDS.
A four-year, $ 1.029 million grant from the National Institutes of Health will support Barkley's work in a new area of AIDS research that examines the chemical processes between the two pieces of reverse transcriptase (RT) protein that mobilizes the HIV-1 virus into action.
For the more than 40 million humans suffering worldwide from AIDS, researchers like Barkley, the M. Roger Clapp University Professor in Case's College of Arts and Sciences, offer hope in finding new therapies for their disease by understanding the basic science of how the AIDS virus HIV-1 functions.
But Barkley is finding that the protein in this virus is not acting like other proteins she encounters in her lab. The flexibility of the AIDS virus that robs humans of their immune defenses has stumped her time and again.
A pilot study in 2003-04 from the American Foundation for AIDS Research provided the groundwork that led to her recent award from the NIH's National Institute of General Medical Sciences.
Barkley's lab is taking a new approach to studying the enzyme RT that copies the viral RNA into the virus' DNA that is then inserted into the human host cell's chromosomal DNA by another HIV-1 enzyme called integrase.
Thousands of journal papers over the past decades have mostly examined the catalytic activity of the HIV-1's RT enzyme and its end products.
Barkley said researchers assumed the RT was like a rock where the two pieces or subunits of the RT protein clung together in order for it to be able to copy the RNA into DNA.
Some of the current drugs called nonnucleoside RT inhibitors used by doctors to treat HIV-1 target the enhancement or lessening of the two subunits of proteins coming together.