Findings help understand how molecules assemble and how the pathogen evades human immune system, according to Nature paper.

Investigators at the Scripps Research Institute have revealed how a critical piece of the Ebola virus is assembled. They were able to determine the structure of the Ebola virus spike protein, which is necessary for entry into human cells, bound to an immune system antibody acting to neutralize the virus.

The structure of the antibody together with the viral glycoprotein helps understand the mechanisms by which the molecules assemble on the viral surface and helps explain how the pathogen evades and exploits the human immune system, according to the scientists.

Besides these results being used in further research related to Ebola and treatments for the disease, they also have implications for the study of viruses in general. “This structure now provides templates by which researchers studying other viruses could try to understand how their virus’ surface protein is assembled and neutralized by an antibody,” according to Ollmann Saphire, leader of the five-year effort. “Structures of the native, oligomeric forms of viral glycoproteins as they exist on the viral surface are exceedingly difficult to achieve and thus exceedingly rare.”

In this study, the antibody bound to the Ebola virus spike protein was reportedly derived from bone marrow of one of the few survivors of the 1995 Ebola outbreak in Kikwit, Democratic Republic of the Congo.

The research is published in the july 10 issue of Nature.

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