Researchers are now a step closer to conquering the ebola virus after recently uncovering the structure of a key part of the Ebola protein - the VP35.
VP35 interferes with the natural resistance of host cells against viral infections.
"Usually when viruses infect cells, the host immune system can fight to eventually clear the virus. But with Ebola infections, the ability of the host to mount a defence against the invading virus is lost," said Gaya Amarasinghe, an assistant professor in biochemistry, biophysics and molecular biology, who led the study.
He explained that this is because the VP35 protein interferes with the host's innate immune pathways that form the first line of defence against pathogens.
In the research, scientists wanted to understand host-viral interactions and thus used a combination of X-ray crystallography and nucleic magnetic resonance spectroscopy to solve the structure using non-infectious protein samples.
nd as the structure from a key part of VP35 is now known, the information can be used as a template for anti-viral drug discovery.
"The next step is to use this structure to identify and design drugs that potentially bind with VP35," he said.
By finding a drug that inhibits VP35 function, it is possible to neutralize the Ebola virus.
"Without functional VP35, the Ebola virus cannot replicate so it is noninfectious," said Amarasinghe.
The Ebola virus can cause hemorrhagic fever that is usually fatal.
The findings of the study are published in the journal Proceedings of the National Academy of Sciences of the United States of America.