In the Field
How to Neutralize a Virus
Laura Walker creates antibody treatments for COVID-19 — and beyond
In the fight against COVID-19, public attention has largely focused on vaccines. But researchers around the world have been racing to find treatments, too. One treatment option is the use of monoclonal antibodies, laboratory-designed proteins that create an efficient and powerful virus combatant.
As the chief scientific officer at biotech company Adagio Therapeutics, Laura Walker BS’07 helped develop a monoclonal antibody for the new coronavirus. “The treatment works against the current version of the virus but also the other viruses in the family that are out there now — and could be in the future,” she says.
Walker’s interest in science is perhaps genetic. Her father was a professor of neuroscience at Brown University. But when she decided to major in biology or chemistry, he encouraged her to look at big state schools “with lots of funding for science,” she says.
Eventually, she chose UW–Madison, where she pursued a biochemistry degree at CALS. She followed up with a Ph.D. from The Scripps Research Institute and a postdoc at the University of California, San Francisco.
Her post-baccalaureate work focused on antibody response to viral pathogens. That led her to an antibody discovery company called Adimab, which she describes as doing “academic research in an industry setting.” Adimab recently launched Adagio Therapeutics to manufacture monoclonal antibodies, and they put Walker in charge of its scientific operations.
“[Walker] has the ability to distill down large volumes of complex information and to know what important questions remain to be answered,” says Adimab chief scientific officer Eric Krauland. “You’ll oftentimes see scientists that are more ‘thinker’ and others that are more ‘doer.’ Laura is a rare combination of both.”
To develop monoclonal antibodies for the new coronavirus, Walker and her team worked with a blood sample from a survivor of severe acute respiratory syndrome coronavirus (SARS-CoV), which was responsible for a global epidemic in 2002-04. It’s a suitable place to start because 80% of the protein spike of the SARS-CoV virus is the same as that of the new coronavirus (SARS- CoV-2) that causes COVID-19.
Antibodies from the SARS-CoV survivor were “broadly neutralizing, but their potency was modest” against COVID-19, Walker says. They sampled every amino acid at every position across the antibody gene to see if they could manipulate it to work better. Eventually, they devised a monoclonal antibody that is 100 times more effective at neutralizing COVID-19.
The practical use of the antibody will depend on how many people choose to be vaccinated for COVID-19 and how well the vaccines perform. If vaccines only provide protection for a year or don’t work well for certain populations, such as the elderly or immunosuppressed, then the antibody could become a competitive option, Walker says. The antibody could also be used as a prophylactic if administered to someone who is not vaccinated but has a known exposure. And it may be needed if the virus mutates beyond the powers of the vaccines or a similar virus emerges from animals again in the future.
“We already know there are many different SARS-related viruses circulating in bat reservoirs; it’s only a matter of time before we see the next one,” Walker says. “Having a broad-spectrum antibody in our toolbox will be important to help mitigate the next coronavirus outbreak.”