Viruses are masters at entering our cells thanks to special proteins that coat their surfaces. When scientists design vaccines, they often create versions of these viral surface proteins to study how the immune system responds. But these lab-made proteins usually lack key parts found within the virus’s membrane, so they don’t necessarily behave like real viruses. This has made it difficult to understand how antibodies actually identify and neutralize these viral targets.
Now, Scripps Research scientists, in collaboration with IAVI and other research institutions, have developed a platform that allows researchers to study viral surface proteins in a more natural-looking way. The new approach uses nanodisc technology, in which these proteins are embedded in particles made of lipid molecules and stored in a membrane-like structure. This could help guide vaccine research by better understanding how antibodies and viral proteins interact.
outlined in nature communications On February 10, 2026, the platform was tested using proteins from HIV and Ebola. These two viruses have long posed a challenge for vaccine developers because the immune system has difficulty effectively targeting their surface proteins. However, this approach could be broadly applicable to other viruses with similar membrane-embedded proteins, such as influenza and SARS-CoV-2.
For many years, we have had to rely on versions of viral proteins that are missing important parts. Our platform allows us to study these proteins in an environment that better reflects their natural environment. This is critical if you want to understand how protective antibodies recognize viruses. ”
William Sieff, co-senior author, professor at the Scripps Research Institute, and executive director of vaccine design at the IAVI Center for Neutralizing Antibodies
In real viruses, surface proteins are not floating, but are embedded in lipid membranes and arranged in a specific shape. However, in most laboratory studies, the membrane anchoring region is removed to facilitate protein production and analysis. Although these shortcuts are convenient, they can obscure important features, especially for antibodies that target regions near the bases of proteins close to the viral membrane.
To address this, the research team assembled vaccine candidate viral proteins into nanodiscs. Nanodiscs are small, stable patches of membrane that hold proteins in place. These lipid discs mimic the outer layer of the virus and help preserve how antibodies identify proteins within the actual virus. Their new platform allows researchers to use a wide range of standard vaccine development tools, including antibody binding testing, immune cell sorting, and high-resolution imaging.
“Integrating all these components into one reliable system was key,” said first author Kimmo Rantalainen, a senior scientist in the Seeff lab. “The individual parts already existed, but making them work together in a reproducible and scalable way opens up new possibilities for how vaccines can be analyzed and designed.”
Using HIV as a test case, the team focused on conserved regions of the virus’s surface proteins near the membrane. This region is targeted by a class of antibodies that can block nearly all HIV variants. Because these antibodies recognize similar parts of the virus even when they mutate, scientists hope that vaccines could eventually trigger an immune response.
Using the Nanodisc platform, the researchers were able to obtain detailed structural snapshots of how these antibodies interact with viral proteins in the membrane context, revealing features not visible when studying the proteins alone. These insights also help explain how certain antibodies neutralize viruses by destabilizing the protein structures they use to infect cells, providing clues about how future vaccines can better engage similar immune responses.
“This structure gives us a level of detail that was previously inaccessible,” Rantalainen said. “It showed new interactions at the membrane interface and suggested why they are important for antibody function.”
To demonstrate that this approach is not limited to HIV, the research team also applied the Nanodisc platform to Ebola proteins and confirmed that antibodies can identify and bind to these proteins in the same membrane-like environment.
Beyond structural studies, this platform can also be used to analyze immune responses to vaccine candidates. Using nanodiscs as molecular “decoys” allows researchers to isolate and study cells that recognize viral proteins, giving them a clearer picture of how the body responds to a particular vaccine candidate. Additionally, the system is scalable, meaning that what previously took more than a month to prepare can now be completed in about a week, making it practical for side-by-side comparisons of multiple candidate designs.
Although this platform is not a vaccine itself, scientists can use it as a tool to inform and accelerate vaccine research, especially for viruses where traditional approaches are inadequate.
“This gives the field a more realistic and accurate way to test ideas at an early stage,” Seef emphasizes. “By improving the way we study viral proteins and antibody responses, we hope this platform will help advance next-generation vaccines against the world’s most challenging viruses.”
sauce:
Scripps Research Institute
Reference magazines:
Rantalainen, K. others. (2026). Viral glycoprotein nanodisc platform for vaccine analysis. nature communications. DOI: 10.1038/s41467-026-68985-1. https://www.nature.com/articles/s41467-026-68985-1
