Researchers at Purdue have recently discovered that the introduction of mutations at certain amino acids along the stretch of VP40, an Ebola envelope protein, can vastly diminish the virus’ ability to enter and replicate in new cells. While this may come at no surprise considering envelope proteins usually allow for viral entry and exit from the cell, the dynamics of this experiment shed light on the way structure and overarching functions of VP40 in Ebola infection. More specifically, it was found that the shape of VP40 may change depending on where in the viral lifecycle it is, most likely due to pH differences in the cell. More importantly, it was shown to be in a monomer, dimer, or octamer in cells, with the octamer being a better tropogen for phosphatidylserine, a lipid on the cell membrane. Mutations to the protein make VP40 more likely to be in the less effective dimeric or monomeric forms on the viral envelope, which translates to a diminished ability for the virus to infect the cell. Moving forward, such studies show that VP40 may be a good target for therapeutics against Ebola because it seems to be so integral to viral replication throughout the cycle.
-Andrew
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