Assembly of the Ebola Virus Nucleoprotein from a Chaperoned VP35 Complex

• Published in: Cell reports (Cambridge) Vol. 12; no. 1; pp. 140 - 149
• Main Authors: Kirchdoerfer, Robert N., Abelson, Dafna M., Li, Sheng, Wood, Malcolm R., Saphire, Erica Ollmann
• Format: Journal Article
• Language: English
• Published: United States Elsevier Inc 07.07.2015; Elsevier
• Subjects: Amino Acid Sequence; Binding Sites; Molecular Sequence Data; Nucleoproteins - chemistry; Nucleoproteins - metabolism; Protein Binding; Protein Multimerization; Protein Structure, Tertiary; RNA - metabolism; Viral Core Proteins - chemistry; Viral Core Proteins - metabolism

Ebolavirus NP oligomerizes into helical filaments found at the core of the virion, encapsidates the viral RNA genome, and serves as a scaffold for additional viral proteins within the viral nucleocapsid. We identified a portion of the phosphoprotein homolog VP35 that binds with high affinity to nasc...