An ebolavirus protein adopts drastically different conformations (pictured) throughout its life cycle, allowing the deadly virus to do more with fewer genes.

Credit: CHRISTINA CORBACI, ZACHARY BORNHOLDT, ERICA OLLMANN SAPHIRE/TSRI

Ebolaviruses kill up to 90% of the people they infect. Erica Ollmann Saphire of the Scripps Research Institute in La Jolla, California, and her colleagues used crystallography, biochemistry and microscopy to track the structure of VP40, a protein that controls ebolavirus assembly and exit from host cells. They learned that the protein does not travel alone as previously thought, but moves to the cell membrane in butterfly-shaped pairs, which then align end-to-end into hexamers that form filaments essential for viral assembly and release. The team also analysed requirements for VP40 to form yet another structure, a previously observed ring that binds to RNA and regulates viral genes in infected cells.

Cell 154, 763–774 (2013)