Characterization of oligomerization of a peptide from the ebola virus glycoprotein by small-angle neutron scattering
- Ministry of Health of the Russian Federation, Research Institute of Influenza (Russian Federation)
- Joint Institute for Nuclear Research (Russian Federation)
- National Research Center “Kurchatov Institute”, Konstantinov Petersburg Nuclear Physics Institute (Russian Federation)
Transmission electron microscopy (TEM) and small-angle neutron scattering (SANS) studies showed that model peptides QNALVCGLRQ (G33) and QNALVCGLRG (G31) corresponding to region 551–560 of the GP protein of the Sudan Ebola virus are prone to oligomerization in solution. Both peptides can form amyloid-like fibrills. The G33 peptide forms fibrils within one day of incubation, whereas the fibrillogenesis of the G31 peptide is observed only after incubation for several months. The possible role of the observed processes in the pathogenesis and the possibility of applying a combination of the TEM and SANS techniques to search for new compounds that are able to influence the protein oligomerization are discussed.
- OSTI ID:
- 22471918
- Journal Information:
- Crystallography Reports, Vol. 61, Issue 1; Other Information: Copyright (c) 2016 Pleiades Publishing, Inc.; Country of input: International Atomic Energy Agency (IAEA); ISSN 1063-7745
- Country of Publication:
- United States
- Language:
- English
Similar Records
Chimeric human parainfluenza virus bearing the Ebola virus glycoprotein as the sole surface protein is immunogenic and highly protective against Ebola virus challenge
Human transbodies to VP40 inhibit cellular egress of Ebola virus-like particles