Great. I know we've only got a couple of minutes left, but I wanted to ask about your COVID efforts. You obviously had a very successful antibody that really helps mitigate some of the morbidities at the height of the pandemic. We're all here now unmasks. Obviously, we've come a long way since then, but there's always a threat of a mutation and an outbreak kind of lurking around the corner. Can you talk about the process by which you were able to find a conserved epitope for COVID, what you've observed preclinically. It looked like from some of the recently published patent filings, you see good binding connects and consistent neutralization potency across a lot of different tested COVID variants. I'm curious, the next steps for your lead compound there or lead antibody there 14287 enters the clinic mid this year.
And I guess, how you discovered it and what you think the challenges might be now from this point forward, where we are in the pandemic to develop a COVID antibody and sort of generate the same sorts of returns that you've got in the past?
Christos Kyratsous
Right. So the process here is very similar to what I think Aris was describing for genetic diseases where you rely on a huge data set of sequences to try and understand patterns, right. So it's the same thing that you are trying to do when you are starting virus evolution. And what we've learned is that over the last more than two years now of available sequences of the virus, you can see that there are certain regions of the virus that are changing very, very frequently for the virus to evolve spread faster amongst the population, but also as a result of the immune pressure.
All of us, when we are vaccinated on where we are infected – the majority of the antibodies that we are developing are against this region of the virus that is called the receptor binding domain. They are very potent neutralizing antibodies. They block the virus very, very well. But also the problem is that this is the region of the virus that is changing very frequently.
So the clinical development of these antibodies is very challenging because you are basically chasing an ever evolving target. It's very difficult. So what we were able to do is we were able to identify sequences that over the multiple years of the evolution of the virus did not change very much or didn't change at all, and then we were able to isolate antibodies against those sequences.
And out of those antibodies, we only chose the ones that are very potent, as potent as the antibodies that are targeting the receptor binding domain, and we chose one, the one that you mentioned as the one that is going to be our clinical candidate. The antibody has been scaled up, and we've already discussed all these things with the regulatory agencies. We are going to be in the clinic in the next few months. And we are hoping that by the end of the year, we are going to start collecting data as these antibodies being tested in patients.
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