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Foot soldiers of the immune system
Date:1/13/2013

tinguishes viral RNA from the RNA found in the human host. During this time, the receptors of the innate immune system are usually able to detect the foreign molecules from the virus and turn on signaling cascades in the cell that leads to the switching on of an antiviral program, both within the infected and nearby uninfected cells. Hundreds of different proteins are produced as part of this anti-viral program, which work in concert to resist the viral infection.

In the Nagar lab, McGill graduate student Yazan Abbas used an arsenal of biophysical techniques, most notably X-ray crystallography, to capture the IFIT protein directly in the act of recognizing the foreign RNA. The work shed light on the interaction between IFITs and RNAs. The researchers determined that IFIT proteins have evolved a specific binding pocket, chemically compatible and big enough to fit only the triphoshorylated end of the viral RNA. Human RNA is not able to tightly interact with this pocket, thereby circumventing autoimmune reactions.

"Once the IFIT protein clamps down on the viral RNA, the RNA is then presumably prevented from being used by the virus for its own replication," says Superti-Furga, "Since many viruses, such as influenza and rabies, rely on triphosphate RNA for their lifecycle, these results have widespread implications in understanding how our cells interact with viruses and combat them."

This work could help advance the development of new drugs for combating a wide array of immune system disorders. "Our findings will be useful for the development of novel drugs directed at IFIT proteins, particularly in cases where it is necessary to dampen the immune response, such as inflammation or cancer therapy," says Nagar.


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Contact: Cynthia Lee
cynthia.lee@mcgill.ca
514-398-6754
McGill University
Source:Eurekalert

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