X-Ray Crystallography of Hanta Virus Protein Reveals Targets for Drug Design

Bank voles are small rodents that are not dangerous by themselves, but their excreta can contain one of the dangerous hantaviruses. While bank voles are unaffected by the infection, hantaviruses can cause potentially fatal diseases in humans for which no treatments exist. In central and northern Europe, infection is accompanied by fever, headache, or even renal failure. The strain that occurs in East Asia -- the Hantaan virus -- is even more dangerous: up to five percent of infected patients die of hemorrhagic fever, renal failure, or severe respiratory disorders. Dr. Daniel Olal and Dr. Oliver Daumke of the Max Delbruck protein is therefore an ideal target structure for future drugs. "Our structure could be useful for Center (MDC) for Molecular Medicine in Berlin have now analyzed the nucleoprotein of the Hantaan virus by means of X-ray crystallography and identified its three-dimensional structure. Dr. Olal and Dr. Daumke have worked out how individual nucleoproteins oligomerize in the presence of RNA molecules, and they have found hexameric circular complexes. "We already know about cellular defense mechanisms that inhibit viral growth. We think that the circular structures we have identified could play a part in this," says Dr. Olal. The nucleoprotein plays an important part in replication of the viral genome. If its function is disrupted, the cell cannot produce functional virus particles. This the design of small molecules that specifically block the nucleoprotein," says Dr. Olal. The researchers have identified three binding pockets on the surface of the protein that could serve as docking sites for such compounds. The new work was reported online on February 25, 2016 in the journal Cell Reports.
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