NEW YORK (June 15, 2012) -- Researchers at Weill Cornell Medical College have unlocked the structure of a key protein that, when sensing certain viruses and bacteria, triggers the body's immediate immune response.
In the journal Molecular Cell, scientists describe the double wing-like crystal structure of this key protein, known as STING, which is a soldier on the front-line of the body's defense against pathogens. Researchers also show STING in action, displaying evidence of a bacterial infection -- an action that launches the body's innate immune response.
"Activation of STING is crucial to the ability of the human body to pick out bits of molecules secreted by pathogens, including many different viruses and bacteria, and alert the human body that they are there. By solving the structure of this protein, we now know how they do this crucial task," says the study's lead author, Dr. Qian Yin, a postdoctoral associate in the laboratory of Dr. Hao Wu, professor of Biochemistry at Weill Cornell Medical College.
"The STING structure provides a remarkable example of the pathogen-host interactions in which a unique microbial molecule directly engages the innate immune system," says Dr. Wu, the study's senior investigator and director of the Lab of Cell Signaling at Weill Cornell.
While the findings have no immediate clinical significance, they might be useful in helping to make vaccines against pathogens more effective. "Based on the structure we have of STING interacting with molecules secreted from bacteria, we may be able to design new molecules that induce a stronger, more persistent immune response," says Dr. Yin.
STING's wings and tail respond to invaders
All plant and animal life use an innate immune response to recognize and respond to an assault by pathogens. This primitive response is immediate, but not long-lasting or protective; the secondary, adaptive immune response sets up the long-term defen
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New York- Presbyterian Hospital/Weill Cornell Medical Center/Weill Cornell Medical College