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William Jewell professor collaborates on anthrax research with KUMED
Contact: Rob Eisele816-415-7574
August 22, 2008

Dr. Scott Falke, assistant professor of biology at William Jewell College, is a member of a collaborative research team studying the structure of anthrax toxin that may one day result in a vaccine to protect humans from lethal anthrax infection.

Dr. Falke is a member of the research team led by Dr. Mark Fisher, professor of biochemistry and molecular biology at the University of Kansas Medical Center. The team’s findings were recently published in the journal Nature Structural & Molecular Biology. Also collaborating on the study were researchers from Harvard University and the University of Missouri-Kansas City.

Although it is known that the anthrax toxin consists of three protein components, no one knew the structure of the protective antigen pore protein component (what the pore actually looks like). The protective antigen pore protein of anthrax toxin is responsible for delivering the other two anthrax toxins into human cells, which leads to cell death.

“Solving the structure is an important step in understanding how the pore facilitates transfer of toxins into the cell,” Dr. Falke said. “Understanding the structure of the pore gives us new insight into the molecular details of anthrax toxicity.”

Presently, the only way to prevent an infection is a vaccine, and it is only approved for use by people at risk of exposure to spores, primarily military personnel and workers in certain research or agricultural jobs.

“From a drug discovery standpoint, understanding the molecular details of anthrax toxins are essential in eventually preventing anthrax infections from harming humans,” said Dr. Mark Fisher, leader of the University of Kansas Medical Center-based research team. “Finding drugs that can prevent this newly discovered structure from forming or blocking the transport of lethal proteins could prevent general anthrax toxicity and will serve as a first line-of-defense for people who acquire an anthrax infection.”

The research team used GroEL, a known “chaperone” protein, to stabilize the protective antigen pore structure so that it could be observed using electron microscopy. Electron microscopy revealed that the protective antigen pore protein forms a syringe-like structure that enables it to “inject” the anthrax toxic proteins into human cells.

“Using GroEL as a scaffold for solving a membrane protein structure may be a useful approach for determining the structure of other membrane-inserted bacterial toxin proteins by electron microscopy,” said Dr. Falke. “I would like to thank Dr. Fisher at the University of Kansas School of Medicine and Dr. Gogol at the University of Missouri-Kansas City for including me as a member of their research team. Collaborative efforts with other Kansas City institutions provide excellent research opportunities for Jewell students.”
 
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