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Emerging subtypes of influenza A virus have many worried about the possibility of an imminent flu epidemic, with the disease's resistance to existing preventive and treatment methods only compounding those fears.
But one Brown student is helping opened a new window of opportunity for designing drugs that can better target the influenza virus.
Anna Levine '08 has worked with a team of researchers at the University of Pennsylvania School of Medicine, which announced last week the discovery of the essential structure of the viral protein M2, the molecular receptor of preventive drugs.
Levine "played a pivotal role" throughout the project, said project leader Bill DeGrado, professor of biophysics and biochemistry at Penn's med school.
Previous influenza drugs had targeted parts of the same viral protein. But those have now mutated, essentially blocking the drugs and rendering them ineffective, Levine said. The goal of the project she participated in - "many, many years" in the making - was to identify a potential target in an essential part of the protein's structure that could not adapt to drugs and develop a resistance, she said.
"Now we know where the sweet spot is," DeGrado said, referring to a molecular channel in the viral protein that new drugs might target.
Levine got involved in the project after doing research at DeGrado's lab during the summer after her freshman year. She said she started out learning the basics of lab work and experimenting with proteins, and eventually came to spend a majority of her summer and winter breaks working on the project.
DeGrado said Levine joined his team at a crucial juncture. At the time, influenza drugs were growing so ineffective that some were pulled off the market, generating a widespread sense of urgency for researchers to pin down the structure of the viral protein. Levine helped to jump-start a push in that direction, DeGrado said.
The process used to determine the viral protein's structure - x-ray crystallography - is like "looking at a rainbow to learn about prisms," Levine said. By bombarding crystallized forms of the protein with intense radiation, her team deduced the molecule's structure.
Such methods can be tedious, Levine said, noting that the process often boils down to trial and error.
"Because the end had so much potential, it drove us not to give up," Levine said. "The gravity of the work and its implications were really exciting."
DeGrado echoed Levine's excitement for the implications of the project's results, especially considering the project's painstaking nature.
"It's been sort of a long slog," he said.
The work Levine did in the Penn lab will also serve as her senior thesis in chemistry. Though she hasn't written a word yet, the fact that the research is complete has her comfortably confident that she will pull it all together, she said.
Now, DeGrado and his team will work to design synthetic compounds that can effectively neutralize the viral protein, Levine said. But the satisfaction of having a final product - a dynamic treatment for influenza A - will have to wait.
"It's a really long road from this kind of thing to having a drug on the market," Levine said.
As for her future plans, Levine said she would like to explore the intersection between medical research and international health. Though the research she has contributed to is important, she said, it only matters if the results get to the people who need them most. Levine hopes to be a part of this process when she goes to work for the consulting firm McKinsey and Company after graduation.
"I've met a lot of incredible people who care about these issues and have incredible access to the resources for dealing with them," Levine said of her future colleagues.
Because she has invested so much time in the research project at Penn, Levine said that for her, the project's results are accompanied by a bittersweet sense of finality.
"I'm incredibly privileged to have worked on this team," she said. "This is like the biggest thing that's ever happened to me."
