Journal: Nature Communications
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A portal into drug design for Epstein–Barr virus
© KATERYNA KON/SCIENCE PHOTO LIBRARY/Getty
A detailed picture of the ring-shaped protein through which DNA from the Epstein–Barr virus (EBV) enters and exits a protective shell could lead to new treatments for the infectious pathogen.
EBV is one of the most common viruses in humans, with about 90% to 95% of all adults infected with it. While it is often present without symptoms, EBV can give rise to glandular fever and various cancers and auto-immune diseases. No drugs are currently licensed for treating EBV infections.
A team that included scientists from the Spanish National Research Council used cryo-electron microscopy to determine the atomic structure of the EBV portal protein to a resolution of 3.5 angstroms.
From above, the protein shows a doughnut-like structure, but from the side, it looks more like a mushroom, with an internal conical channel running through a wider ‘cap’ and narrower ‘stem’.
This map of the virus’ portal protein offers a starting point for drug-design strategies based on structure.
- Nature Communications 10, 3891 (2019). doi: 10.1038/s41467-019-11706-8