Structural and functional basis of VLDLR usage by Eastern equine encephalitis virus. (https://pubmed.ncbi.nlm.nih.gov/38176410/)

These scientists wanted to understand how a virus called Eastern equine encephalitis virus (EEEV) enters our cells and causes illness. They focused on a protein called very-low-density lipoprotein receptor (VLDLR) that helps the virus get inside our cells.

To study this, the scientists used a special microscope called cryo-electron microscopy to take pictures of the virus and the VLDLR protein together. They also made changes to the virus and the protein to see how it affected their interaction.

What they discovered was that the virus uses different parts of the VLDLR protein to attach to multiple parts of itself at the same time. This helps the virus enter our cells more effectively. They also found that no single part of the VLDLR protein is enough to support the virus's entry.

They also noticed that while most strains of the virus have two sites on the VLDLR protein that they can attach to, one particular strain called EEEV PE-6 has a change in its structure that allows it to attach to an additional site on the VLDLR protein.

Using all this information, the scientists were able to create a special decoy receptor that looks like the VLDLR protein but doesn't let the virus enter our cells. They tested this decoy receptor on mice and found that it protected them from getting sick when they were exposed to the virus.

In conclusion, these scientists studied how the EEEV virus interacts with the VLDLR protein to enter our cells. They discovered how the virus attaches to different parts of the protein and used this knowledge to create a decoy receptor that can prevent the virus from causing illness.

Adams LJ., Raju S., Ma H., Gilliland T Jr., Reed DS., Klimstra WB., Fremont DH., Diamond MS. Structural and functional basis of VLDLR usage by Eastern equine encephalitis virus. Cell. 2024 Jan 18;187(2):360-374.e19. doi: 10.1016/j.cell.2023.11.031. Epub 2024 Jan 3.