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Publication Abstract from PubMed

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 A) 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.

High-resolution Crystal Structure of Dimeric VP40 From Sudan ebolavirus.,Clifton MC, Bruhn JF, Atkins K, Webb TL, Baydo RO, Raymond A, Lorimer DD, Edwards TE, Myler PJ, Saphire EO J Infect Dis. 2015 Oct 1;212 Suppl 2:S167-71. doi: 10.1093/infdis/jiv090. Epub, 2015 May 9. PMID:25957961^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.