When the Hippo pathway is “off,” the downstream protein YAP (red) is localized to the nucleus. VP40 (cyan), a viral matrix protein found in the Ebola virus, simultaneously drives vigorous formation and egress of virus-like particles along the cell periphery. In addition, Ebola virus nucleoprotein directs the formation of cytoplasmic inclusion bodies (yellow), also known as viral factories, in which viral RNA synthesis (transcription and replication) occurs. (Image: Courtesy of Ronald Harty)
Mortality rates from Ebola outbreaks can be as high as 90%, according to the Centers for Disease Control and Prevention, and 55 people died in the most recent outbreak in Uganda in 2022. The virus continues to evolve, but currently approved vaccines and therapeutics remain limited. And Ronald N. Harty, professor of pathobiology and microbiology at the University of Pennsylvania School of Veterinary Medicine, and Jingjing Liang, a research associate in the Harty Lab, still have a lot of questions.
How would currently approved vaccines fare if the virus were to spread widely? Why, in central Africa where Ebola outbreaks occur, is the virus able to persist in fruit bats as a natural reservoir, instead of killing them like it kills humans? How is the virus able to sometimes stay dormant in different types of tissues for weeks, months, or even years before it starts replicating again, only then causing symptoms and potentially death?
Harty has been working on Ebola for more than two decades. In trying to better understand virus-host interactions to identify better treatments, he has focused on VP40, the viral matrix protein that plays a critical role in how the virus escapes from a cell. His lab has looked at key pieces of this protein, including the L domain, a short stretch of amino acids that hijacks host proteins the Ebola virus uses to exit the cell.
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