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Hidden weak spots in HIV and Ebola revealed with breakthrough nanodisc technology

A new “nanodisc” technology lets scientists see viruses as they truly are—opening the door to smarter, more powerful vaccines.

Date:

April 12, 2026

Source:

Scripps Research Institute

Summary:

A new nanodisc-based platform lets scientists study viral proteins in a form that closely mimics real viruses, revealing how antibodies truly recognize them. This approach uncovered hidden interactions in viruses like HIV and Ebola that traditional methods missed. By recreating the virus’s membrane environment, researchers can better understand how immune defenses work. The technique could speed up the development of more effective vaccines.

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Researchers have developed a nanodisc system that recreates viral proteins in their natural membrane environment, exposing how antibodies actually attack viruses. Credit: Shutterstock

Viruses are highly effective at entering human cells, largely because of specialized proteins that cover their outer surfaces. These proteins are key targets in vaccine development. To study them, scientists typically create lab versions to see how the immune system might respond. However, these simplified versions often leave out important sections that normally sit within the virus's outer membrane. As a result, they do not always behave the same way they would in a real infection, making it harder to understand how antibodies truly recognize and stop viruses.

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 much more natural form. Their method uses nanodisc technology, which places the proteins into tiny particles made of lipids. This setup mimics the virus's outer membrane, helping preserve the proteins' natural structure and behavior. The approach offers a clearer view of how antibodies interact with viruses and could help guide future vaccine design.

Nanodisc Technology Mimics Viral Membranes

The study, published in Nature Communications, tested the platform using proteins from HIV and Ebola. These viruses have long posed challenges for vaccine development because their surface proteins are especially difficult for the immune system to target. The researchers believe the same method could also be applied to 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."

In real viruses, surface proteins are embedded within a lipid membrane and arranged in specific shapes. In contrast, most laboratory studies remove the membrane-anchoring portion to make the proteins easier to handle. While this simplifies experiments, it can hide important details, especially for antibodies that target regions near the base of the protein close to the membrane.

To overcome this limitation, the team incorporated vaccine candidate proteins into nanodiscs. These small, stable lipid patches hold the proteins in place and closely resemble the virus's outer layer. This setup allows scientists to study how antibodies interact with proteins in a more realistic context. The platform also supports standard vaccine research tools, including antibody binding tests, immune cell sorting and high-resolution imaging.

"Putting all of these components together into a single, reliable system was the key," says first author Kimmo Rantalainen, a senior scientist in Schief's lab. "The individual pieces already existed, but making them work together in a way that's reproducible and scalable opens up new possibilities for how vaccines are analyzed and designed."

New Insights Into Antibody Responses

Using HIV as an example, the researchers focused on a stable region of the virus's surface protein located near the membrane. This region is targeted by a group of antibodies that can block a wide range of HIV variants. These antibodies recognize parts of the virus that remain consistent even as it mutates, making them especially valuable for vaccine research.

With the nanodisc platform, the team captured detailed structural views of how these antibodies interact with viral proteins in their natural membrane environment. This revealed features that cannot be seen when proteins are studied in isolation. The findings also shed light on how certain antibodies may neutralize viruses by disrupting the structures they use to infect cells, offering useful clues for desig