“Our ultimate goal here is to obtain structural information on antibodies and their binding sites, and use that to guide SARS-CoV-2 vaccine design, just as our lab has done with influenza and HIV,” says the study’s co-first author Nicholas Wu, PhD, a postdoctoral research associate in the Wilson lab.
The new study centers on an anti-SARS-CoV antibody called CR3022 that was originally isolated in 2006 by the pharmaceutical company Crucell Holland B.V. in the Netherlands. A report from Chinese scientists earlier this year indicated that CR3022 cross-reacts against SARS-CoV-2. Wilson’s team used their structural mapping expertise to determine how the antibody binds to SARS-CoV-2.
A key finding is that the antibody’s binding site is highly similar between the two coronaviruses—differing by just four protein building blocks called amino acids. That high degree of similarity implies that the site has an important function that would be lost if it mutated significantly.
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