A viral infection can be hard to diagnose and treat.
That makes it hard to track who is at risk for infection and how to treat it.
But scientists are starting to see promise in developing new drugs that can be administered to humans and animals and to humans with the virus.
To get there, we need to find a way to understand what triggers the symptoms of a viral infection.
It’s a big challenge.
But there are ways to identify viral proteins and how they interact with other molecules.
We can even look for a gene in the virus that causes a protein to be expressed by a specific cell type.
If we can figure out what triggers a virus to produce proteins, we can target the right molecule to treat the virus in the right way.
That’s the goal of a new project by scientists at the National Institutes of Health, the University of Texas MD Anderson Cancer Center and the National Center for Biotechnology Information (NCBI).
Their new drug, an antibody called CCL-4, targets a protein in the viral genome called an exonuclease.
That exonuclelease is responsible for breaking down viral proteins into their building blocks, and its activity is activated when the viral protein is disrupted.
CCL4’s effect on exonutases is similar to the effect of chemotherapy drugs.
But the exonulease’s action is much stronger, so the antibodies’ antibodies target it in a more targeted way.
“We were surprised to see that the exons of viral proteins are very similar to those of genes,” said John C. Pappas, PhD, a postdoctoral researcher at NCBI and lead author of a paper describing the work in Nature.
“That means we have some idea of what proteins are made of, and it may give us some insight into how viral infections arise.”
It’s possible that CCL.4 could someday be used to target a variety of viral genes and disrupt them in a way that stops them from producing proteins that are harmful.
But that would require finding a way for the exonic proteins to cross the blood-brain barrier and infect the brain, Pappans team said.
The new antibody is a proof-of-concept, said David M. Ochsner, PhD and co-first author of the paper.
“This work is an exciting start,” said Ochsen.
But it’s not yet clear if the antibody’s effect will work on all viruses or just some.
In the meantime, the antibody has already been tested in animals, Parnell said.
But Parnells team wants to make sure it works well in humans, too.
“One thing we know about the human immune system is that it doesn’t like to cross into the brain,” he said.
“It would be nice to have a drug that would block that effect.”
In the near future, Pawser said, the team will look at whether the antibody can be used as a therapeutic against viruses like SARS-CoV-2, coronavirus and Ebola.
If it does, the antibodies could be tested on human patients and, eventually, in humans with severe viral infections, said Ochnsner.
The research was supported by the National Science Foundation and the NCBI.
About NCBI: The National Institutes for Health is the largest supporter of basic, clinical, and applied research in the life sciences, including basic, biomedical, translational and population biology.
For more information, visit www.nih.gov.