In the Ebola virus one of the proteins, VP40, has the ability to refold to achieve new functions; three structural forms of VP40 have been determined, with each structure conferring a separate and essential function in the virus life cycle. The image illustrates (top) a butterfly-shaped dimer critical for membrane trafficking; (middle) a rearranged hexameric structure essential for building and releasing nascent virions; (bottom) an RNA-binding octameric ring that controls transcription in infected cells
Bornholdt, T. Noda, D.M. Abelson, P. Halfmann, M.R. Wood, Y. Kawaoka, E. Ollmann Saphire, Cell 154, 763 (2013) [DOI: 10.1016/j.cell.2013.07.015]
Funding Acknowledgements: Beamlines at Argonne National Laboratory’s (ANL) Advanced Photon Source (APS): 19-ID and GM/CA 23-ID; SLAC National Accelerator Laboratory’s (SLAC) Stanford Synchrotron Radiation Lightsource (SSRL): 12-2; and Lawrence Berkeley National Laboratory’s (LBNL) Advanced Light Source (ALS) 5.0.2. E.O.S. support: Career Award in the Biomedical Sciences and an Investigator in Pathogenesis of Infectious Disease Award from Burroughs Welcome Fund, as well as The Skaggs Institute of Chemical Biology and a National Institutes of Health’s (NIH) National Institute of Allergy and Infectious Disease (NIAID) award (R43 AI1088843). Z.A.B. support: grant (2T32AI007244) to The Scripps Research Institute (TSRI; manuscript #21649) Department of Immunology and Microbial Science. Y.K.: membership within and support from the Region V “Great Lakes” Regional Center for Excellence (RCE) for Biodefense and Emerging Infectious Disease Research Program (NIH award U54 AI057153). T.N. support: Grant-in-Aid for Young Scientists from Japan Society for the Promotion of Science and Grant-in-Aid for Scientific Research on Priority Areas from the Ministry of Education, Culture, Sports, Science, and Technology.