Viruses are highly effective at infecting human cells, largely because of specialized proteins that cover their outer surfaces. These proteins are also a key focus for vaccine design. To study them, scientists often create lab-made versions to see how the immune system might respond. However, these simplified versions usually omit important sections embedded in the virus’ membrane. Without those pieces, the proteins do not fully behave the way they do in real viruses, making it harder to understand how antibodies recognize and disable them.

Researchers at Scripps Research, working with IAVI and other collaborators, have now developed a new platform that allows these viral proteins to be studied in a form that closely resembles their natural state. The method uses nanodisc technology, where the proteins are placed into tiny particles made of lipids. This creates a membrane-like environment that better preserves their structure and function. As a result, scientists can gain clearer insights into how viral proteins and antibodies interact.

Nanodisc Technology Improves Vaccine Research
The new platform, described in Nature Communications, was tested using proteins from HIV and Ebola. These viruses have been particularly difficult targets for vaccines because their surface proteins are not easily recognized by the immune system. The researchers say the same approach could also be used to study other viruses with similar membrane-bound proteins, including influenza and SARS-CoV-2.

“For many years, we’ve had to rely on versions of viral proteins that are missing important pieces,” says co-senior author William Schief, a professor at Scripps Research and executive director of vaccine design at IAVI’s Neutralizing Antibody Center. “Our platform lets us study these proteins in a setting that better reflects their natural environment, which is critical if we want to understand how protective antibodies recognize a virus.”