WEST LAFAYETTE, Ind. -- Purdue University scientists have unlocked the secrets of a receptor that the common cold virus uses as an entryway to infect human cells.
Their findings, detailed in the April 14 issue of the Proceedings of the National Academy of Sciences, may help slam the door on one of the most troublesome and universal pathogens known to man.
A research team led by Purdue researcher Michael G. Rossmann reports that it has analyzed in atomic detail the three-dimensional structure of the part of the cellular receptor that binds to a virus that causes the majority of colds in humans.
Knowing the structure of this receptor will help scientists unravel the mystery of how cold viruses enter cells, and it may suggest ways for developing drugs that prevent the common cold and other illnesses caused by similar viral pathogens, says Rossmann, who is the Hanley Distinguished Professor of Biological Sciences.
"By solving the structure of this receptor, we can gain insights into the chemical and biological activity that occurs when a cold virus infects a human cell," he says.
The receptor, called ICAM-1, is made up of a single protein and is shaped somewhat like an arm divided into five sections, or domains, extending from a shoulder that penetrates the cellular membrane. Rossmann's group has solved the structure of the first two domains, which are located at the "hand" end of the molecule where the virus attaches. Each cell may contain thousands of these receptors on its membrane.
Similar results were found by a group directed by Tim Springer at Harvard Medical School, and they appear in the same issue of the journal.
ICAM-1 -- an acronym for intercellular adhesion molecule one -- is one of many types
of adhesion molecules found in multicelled organisms. As the name implies, adhesion
molecules play a role in binding cells to other molecules or cells. ICAM-1 normally
functions to hold infection-fighting white blood cells in
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Contact: Susan Gaidos
susan_gaidos@uns.purdue.edu
765-494-2081
Purdue University
14-Apr-1998