Researchers have determined the crystal structure of the Ebola virus surface protein that binds host cells, they report online today in linkurl:Nature.;http://www.nature.com/nature/index.html The findings open the door to solving the long-standing mystery of the virus's mechanism of infection and designing drugs to combat the deadly hemorrhagic fever caused by linkurl:Ebola.;http://www.the-scientist.com/article/display/22846/ The paper is a "breakthrough," said linkurl:Lijun Rong,;http://www.uic.edu/depts/mcmi/faculty/rong/index.htm an associate professor at the University of Illinois at Chicago who was not involved in the study. People in the field have been looking for this structure for a long time, he emphasized, and the advance is "really exciting for us." Ebola virus is a "clever little thing," said Erica Ollmann Saphire, an immunologist at the Scripps Research Institute and main author of the paper. "It's a tiny stripped-down machine of just seven genes, yet it's able to utterly defeat most defenses we can come up with against it." linkurl:Ollmann...
Image captions and credits: First: Crystals of the Ebola virus glcyoprotein in complex with an antibody from a human survivor. Photo: Jeffrey Lee and Erica Ollmann Saphire, TSRI Second: The GP1 subunits (blue) are tied together by the GP2 subunits (white). A rare human antibody from an outbreak survivor (yellow) bridges the two subunits together. Image: Christina Corbaci and Erica Ollmann Saphire, TSRI The crystal structure of the Ebola virus GP with the putative receptor binding site in pink, sequestered in the bowl of the GP chalice in white. Movie: Erica Ollmann Saphire, TSRI

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