
NIH expected to award Scripps Research nearly $4.2 million over 5 years to advance tools for vaccine design Funding will expand methods for studying viral proteins and immune responses in more realistic settings for HIV and other severe pathogens.
April 10, 2026
LA JOLLA, CA Scripps Research has received more than $500,000 in first-year funding of a five-year R01 grant worth a total of approximately $4.2 million from the National Institutes of Health (NIH) to advance technologies for studying viral proteins and antibody responses, tools that could aid the design of vaccines against deadly pathogens like HIV. The first year of funding totals $511,531, with the NIH expected to provide $918,223 annually in subsequent years, pending the availability of funds.
This award supports efforts to refine and expand platforms that analyze viral proteins in conditions that more closely resemble real viruses. Such approaches move beyond the simplified, truncated versions of proteins typically used in labs.
The goal is to create approaches for observing viral proteins in a context that more closely reflects their natural environment, says principal investigator Kimmo Rantalainen, a senior scientist at Scripps Research. If we can measure how antibodies interact with these proteins more accurately, it becomes easier to evaluate vaccine candidates and understand what kinds of immune responses they produce.
The R01 builds on an NIH bridge award that provided roughly $400,000 in initial support while the full grant application was under review. Bridge programs help maintain momentum between major grants, allowing scientists to further develop promising projects and generate preliminary data needed for long-term support.
The project extends recent work from Rantalainen and colleagues from the labs of Scripps Research professors William Schief and Andrew Ward describing a platform that embeds full-length viral proteins into small, lipid particles known as nanodiscs. This platform enables scientists to study viral proteins as they exist on a virus, attached to the pathogen's membrane. It also preserves key regions that are often missing from lab-made versions of these proteins but are important for how antibodies bind to a virus and block infection.
With the NIH funding, Rantalainen's team plans to apply the nanodisc-based platform to ongoing vaccine projects and expand the methodology in new directions. One area of focus will be adapting the system for electron microscopy-based polyclonal epitope mapping, a technique developed in Ward's lab to visualize how many different antibodies bind to a viral protein at once. This lets scientists see which parts of a virus the immune system targets after vaccination, providing guidance for vaccine design.
Integrating such tactics could help researchers analyze vaccine-induced antibody responses in greater detail, providing insights that could ultimately guide future vaccine strategies. The combination of bridge support and the newly approved R01 will permit Rantalainen and his team to continue refining their methods while applying them to current challenges.
We're using the tools introduced in our latest publication to advance vaccine development, but we're also pushing this approach further, explains Rantalainen. The aim is to make these techniques broadly useful and available to the wider research community so we can better understand what makes a vaccine work.
Immunology & Microbiology
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