Using improved microscope technology, a team including Purdue's Timothy S. Baker and a colleague at Harvard has determined the structure of a reovirus (short for "respiratory enteric orphan" virus) down to the 7.6-angstrom scale, better than twice the 18-angstrom resolution previously available. The newly obtained structure shows not only the molecular composition of the virus but even the position and orientation of those molecules.

"We have visualized the innards of a human reovirus at an unprecedentedly high resolution," said Baker, who is professor of biology in Purdue's School of Science. "We can now look at the components of the viral machine to see how they work, which hopefully will give us insight into how it manufactures the genetic weapons it uses to infect cells."

The reovirus is a member of a viral family that often causes diarrhea in young children. Infections caused by the closely related rotaviruses, for example, are responsible for approximately 1 million deaths annually in developing countries where water shortages can make rehydration difficult for victims.

The research, which appears in the December issue of "Nature Structural Biology," was performed by a team of Purdue researchers, including first author and graduate student Xing (pronounced SHING) Zhang, graduate student Steve Walker, and cryo-microscopist Paul Chipman. The work is part of a long-standing collaborative study of reoviruses with Max L. Nibert of Harvard Medical School's Department of Microbiology and Molecular Genetics.

Reoviruses are members of an unusual viral family, in that they do not simply deposit their genetic material into the victim's cytoplasm, or
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Contact: Chad Boutin
cboutin@purdue.edu
765-494-2081
Purdue University
15-Dec-2003