High-resolution Crystal Structure of Dimeric VP40 From Sudan ebolavirus

• Published in: The Journal of infectious diseases Vol. 212; no. suppl 2; pp. S167 - S171
• Main Authors: Clifton, Matthew C., Bruhn, Jessica F., Atkins, Kateri, Webb, Terry L., Baydo, Ruth O., Raymond, Amy, Lorimer, Donald D., Edwards, Thomas E., Myler, Peter J., Saphire, Erica Ollmann
• Format: Journal Article
• Language: English
• Published: United States Oxford University Press 01-10-2015
• Subjects: Ebola and Marburg Viruses-Research, Outbreak Management, Epidemiology and Ecology; Ebola virus; Ebolavirus - chemistry; Ebolavirus - metabolism; Escherichia coli - metabolism; MOLECULAR BIOLOGY; Protein Multimerization - physiology; Protein Structure, Tertiary - physiology; Solutions - chemistry; Sudan; Viral Matrix Proteins - chemistry; Viral Matrix Proteins - metabolism; Sudan; Ebola virus; Sudan ebolavirus; virus budding; matrix protein; VP40
• ISSN: 0022-1899; 1537-6613
• DOI: 10.1093/infdis/jiv090

Ebolaviruses cause severe hemorrhagic fever. Central to the Ebola life cycle is the matrix protein VP40, which oligomerizes and drives viral budding. Here we present the crystal structure of the Sudan virus (SUDV) matrix protein. This structure is higher resolution (1.6 Å) than previously achievable. Despite differences in the protein purification, we find that it still forms a stable dimer in solution, as was noted for other Ebola VP40s. Although the N-terminal domain interface by which VP40 dimerizes is conserved between Ebola virus and SUDV, the C-terminal domain interface by which VP40 dimers may further assemble is significantly smaller in this SUDV assembly.