Scientists at Scripps Research have developed a nanodisc platform that mimics viral membranes, uncovering hidden interactions in HIV and Ebola proteins that traditional methods miss. The technology allows for more accurate study of antibody responses, potentially accelerating vaccine development. The findings appear in Nature Communications.
Researchers led by William Schief at Scripps Research, in collaboration with IAVI, created nanodiscs—tiny lipid particles that embed viral surface proteins in a setup resembling the viruses' outer membranes. This preserves the proteins' natural structures, unlike lab versions that strip away membrane-anchoring parts and obscure key details near the base. The platform supports antibody binding tests, immune cell sorting, and high-resolution imaging, streamlining analysis from weeks to days. Schief, a professor at Scripps and executive director of IAVI's Neutralizing Antibody Center, said, '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.' Testing on HIV revealed detailed views of antibodies targeting a stable membrane-proximal region, effective against diverse variants by disrupting infection structures. Ebola proteins also bound antibodies effectively in this context. First author Kimmo Rantalainen noted, 'The structure gave us a level of detail we simply couldn't access before,' highlighting new membrane interface interactions. The method extends to viruses like influenza and SARS-CoV-2. While not a vaccine itself, it equips researchers to evaluate candidates more realistically, as Schief emphasized: 'This gives the field a more realistic, accurate way to test ideas early on.' The study, 'Virus glycoprotein nanodisc platform for vaccine analytics,' lists numerous Scripps authors and support from NIH, Gates Foundation, and others.