> In this study, we demonstrated that the VP35 protein of EBOV interacts non-covalently with unanchored K63-linked polyUb chains. This interaction between Ub and VP35 promotes viral polymerase activity leading to optimal virus replication.

> Using a pharmacological approach to block Ub-VP35 interactions, we showed that these interactions are relevant in promoting polymerase activity and replication of infectious EBOV. However, loss of Ub interaction with VP35 did not show a perfect correlation with the reduced polymerase activity and virus replication.

In short, it seems as though the ebola VP35 protein interacts with certain types of ubiquitin proteins (a protein found in most of our cells) and that blocking this interaction with drugs led to reduced but not zero replication. I figure their line of reasoning is to determine which interactions between proteins are crucial and then design some drugs with the help of computation models to severely reduce replication -- so far, no real success but a step in the right direction.

The virus uses a special protein, called VP35, as a tool to help make copies. Now, think of ubiquitin (Ub) as a kind of accessory that can attach to VP35. Scientists found that VP35 likes to hang out with a specific form of Ub, not by sticking directly to it (like glue), but more like holding hands non-covalently, which means they can easily let go of each other. This hand-holding is critical because it helps the virus copy itself more efficiently.

Researchers dove deeper and found exactly how VP35 and Ub hold hands, identifying the exact parts that touch. Knowing this, they looked for and found special molecules that can interrupt this hand-holding, making it harder for the virus to make copies of itself. These molecules act like a wedge to keep VP35 and Ub apart.