Science Daily October 20, 2020
As the world grapples with COVID-19, the Ebola virus is again raging. Researchers at the University of Delaware are using supercomputers to simulate the inner workings of Ebola, observing the way molecules move, atom by atom, to carry out their functions. In the team’s latest work, they reveal structural features of the virus’s coiled protein shell that may be promising therapeutic targets, more easily destabilized, and knocked out by an antiviral treatment. They found that single-stranded viral RNA (ssRNA) is essential for maintaining structural integrity of the nucleocapsid. Other molecular determinants observed to stabilize the nucleocapsid include (nucleoprotein) NP–RNA and NP–NP interactions and ion distributions. Additionally, the structural and dynamical behavior of the nucleocapsid monomer depends on its position in the helical assembly. NP monomers present on the longitudinal edges of the helical tube are more exposed, flexible, and have weaker NP–NP interactions than those residing in the center. The work provides key structural features stabilizing the nucleocapsid that may serve as therapeutic targets…read more. Open Access TECHNICAL ARTICLE