Baric Transcribed Interview (Redacted) — page 125

DC.Scheduling@LexitasLegal.com the most optimal receptor binding domain possible to grab either the human ACE2 receptor or the mouse ACE2 receptor. The thought in the field from him, as a biochemist, was that would be the most optimal and most dangerous form of virus. I disagreed with him, because in reality, biochemical interactions are, in essence, a bell-shaped curve. If they can't interact very well, the virus can't get in. If they react too well, that interaction can't come apart. So the virus can't get in, and the virus, as it tries to release, gets caught up in what's called a dominant negative effect, and it will prevent virus replication. And the reason I knew this is I had overexpressed receptors before, with mouse hepatitis virus. And because there was so much receptor there, the virus, as it got in, it replicated fine, but when it came out all the spikes were stripped off of the particle. So if the interaction is too great it kills the virus. Anyone who might want to do nefarious work in science, wanted to create something, is going to think that the most efficient interaction is where you want to go. So I tested that hypothesis and showed that I was right, that the super-binding things were just as deleterious as the really poor-binding ones. I subsequently told NIH and destroyed those viruses. I have never told anyone, and I would