AI Article Synopsis
- Current COVID-19 vaccines struggle to provide long-lasting immunity against new viral variants, highlighting the need for better vaccine designs.
- The study analyzed the immune responses generated by two original vaccines, mRNA-1273 and NVX-CoV2373, revealing that both induce significant antibody responses primarily targeting the N-terminal domain (NTD) of the Spike protein.
- It was found that the antibodies targeting the NTD supersite are particularly vulnerable to mutations in variants, suggesting future vaccine development should focus on strategies to mask this site to enhance effectiveness against emerging strains.
Article Abstract
Current COVID-19 vaccines are largely limited in their ability to induce broad, durable immunity against emerging viral variants. Design and development of improved vaccines utilizing existing platforms requires an in-depth understanding of the antigenic and immunogenic properties of available vaccines. Here we examined the antigenicity of two of the original COVID-19 vaccines, mRNA-1273 and NVX-CoV2373, by electron microscopy-based polyclonal epitope mapping (EMPEM) of serum from immunized non-human primates (NHPs) and clinical trial donors. Both vaccines induce diverse polyclonal antibody (pAb) responses to the N-terminal domain (NTD) in addition to the receptor-binding domain (RBD) of the Spike protein, with the NTD supersite being an immunodominant epitope. High-resolution cryo-EMPEM studies revealed extensive pAb responses to and around the supersite with unique angles of approach and engagement. NTD supersite pAbs were also the most susceptible to variant mutations compared to other specificities, indicating that ongoing Spike ectodomain-based vaccine design strategies should consider immuno-masking this site to prevent induction of these strain-specific responses.
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|---|---|
| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC11661243 | PMC |
| http://dx.doi.org/10.1101/2024.12.11.628030 | DOI Listing |
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