The Ebola virus (EBOV) causes lethal¹ hemorrhagic fever in humans, with extremely high morbidity² and mortality. It was first discovered in two simultaneous outbreaks near the Ebola River in sub-Saharan Africa in 1976. Sporadic³ outbreaks followed until 2014, when it re-emerged in Western Africa and caused a widespread epidemic⁴. As of 24 April 2015, the World Health Organization (WHO) has reported a total number of 26,101 suspected cases and 10,824 deaths. Despite the high death rate of the Ebola hemorrhagic disease, there are no FDA-approved treatments or vaccines⁵ available to date, nearly 40 years after the initial outbreak. For decades, numerous research works have identified the structures of most EBOV encoded proteins except two, the L protein and nucleoprotein (NP), because of the difficulties they present in the expression, purification and crystallization process. Recently, researchers from Nankai University and the Tianjin International Joint⁶ Academy of Biotechnology & Medicine identified the structure of the EBOV NP core domain⁷ and published their findings in Springer's open access journal Protein & Cell.

 

NP plays the essential role in the EBOV life cycle, by facilitating viral RNA encapsidation to form a ribonucleoprotein complex. The structure of EBOV NP, solved to 1.8 Å resolution, reveals how EBOV NP clamps an RNA binding⁸ groove⁹ between its two lobes¹⁰, which presents similarities with the other reported viral NPs from the Mononegavirales order. This structural¹¹ information should provide valuable insights to help us understand the EBOV genome assembly and transcription mechanism¹². In addition, the researchers identified a highly conserved¹³ hydrophobic groove on the surface of EBOV NP, which provides great potential for the development of antiviral therapies targeting EBOV RNP formation.

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