WASHINGTON, Jan. 12 (Xinhua) -- A team led by Iowa State University scientists has solved the structure from a key part of the Ebola protein known as VP35, which interferes with the natural resistance of host cells against viral infections, the university said Monday.

    "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 defense against the invading virus is lost," said Gaya Amarasinghe, team leader and an assistant professor in biochemistry, biophysics and molecular biology.

    He said that is because the VP35 protein interferes with the host's innate immune pathways that form the first line of defense against pathogens.

    In their research in understanding host-viral interactions, the team employed a combination of X-ray crystallography and nucleic magnetic resonance spectroscopy to solve the structure using non-infectious protein samples.

    Now that the structure from a key part of VP35 is available, the information can be used as a template for anti-viral drug discovery.

    "The next step is to use the structure to identify and design drugs that potentially bind with VP35," Amarasinghe said.

    If a drug that inhibits VP35 function can be discovered, then the Ebola virus could potentially be neutralized.

    "Without functional VP35, the Ebola virus cannot replicate so it is noninfectious," Amarasinghe said.

    A report describing the findings was published this week in the journal Proceedings of the National Academy of Sciences of the United States of America.

    The Ebola virus can cause hemorrhagic fever that is usually fatal. According to the Center for Disease Control and Prevention, outbreaks have caused more than 1,000 deaths, mostly in central Africa, since the Ebola virus was first recognized in 1976.