A new, molecular view of the Ebola virus could hold the key to countering this severe and often fatal disease. NIAID-supported researchers have determined the structure of a critical part of Ebola’s VP35 protein, which interferes with the natural immune response to infection.
Typically, when a virus infects cells, the human immune system responds to the virus’ RNA and mounts a defense. A protein on the surface of the Ebola virus, called VP35, masks the viruses’ RNA, and inhibits the human immune system from attacking the virus.
To learn more about this interaction between the host and the virus, researchers at Iowa State University determined the X-ray crystal structure of a double-stranded Ebola RNA bound to VP35 from the deadly Zaire species. The team, led by Dr. Gaya Amarasinghe, found that multiple copies of VP35 cap the end of the double-stranded RNA and bind to the RNA backbone, preventing host immune systems from recognizing infection.
The findings are similar to those of researchers at The Scripps Research Institute, where the same unusual binding techniques were found in the less-destructive Ebola Reston virus.
Scientists hope to use these insights into the Ebola virus structure and function to develop new treatments. One avenue being explored is development of a drug that targets the VP35 functions and could inhibit RNA binding, preventing severe infection.
Leung DW et al. Structural basis for dsRNA recognition and interferon antagonism by Ebola VP35. Nat Struct Mol Biol. 2010 Feb;17(2):165-72. Epub 2010 Jan 17.
Last Updated August 12, 2010