ArticleResearch square2025
A Computationally Optimised Structural Integrity Sequence Enhances Vaccine Stability, Yield and Safety Profile.
Article in Research square, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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Authors and funding
7 authors.
Funding
Abstract
Recombinant vaccines are a cornerstone of global health, exemplified by the eradication of type 3 wild poliovirus in 2020 due to extensive vaccination campaigns. However, sequence similarity between vaccine antigens and human proteins could theoretically risk autoimmune reactions via molecular mimicry. We present the 'Vaccine Candidate de-Risking and Stabilisation' (VaCRiSta) computational pipeline; integrating sequence similarity searches, epitope prediction, homology modeling, and molecular dynamics simulations to de-risk and structurally stabilize vaccine candidates. As a case study, we applied VaCRiSta to the GCN4 trimerization domain in the context of the mumps F protein. The optimized sequence (GCN4_QM) eliminates 139 7-mer and 50 8-mer human proteome matches, is predicted to enhance stability of the trimeric F protein assembly and doubles protein expression yield (2.2 vs. 1.1 mg/L) for a mumps vaccine candidate. GCN4_QM maintains structural integrity, confirmed by negative-stain electron microscopy, and elicits approximately 3-fold higher neutralizing antibody titers in mice (
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