Structure-directed mutagenesis produces thermostable SARS-CoV-2 spike protein trimers with potential vaccine booster applications biorxivpreprint MonashUni UniMelb TheDohertyInst UNSW mutagenesis SARSCoV2 spike vaccine booster
By Dr. Chinta SidharthanNov 14 2022Reviewed by Danielle Ellis, B.Sc. In a recent study posted to the bioRxiv* preprint server, a team of researchers investigated the change in the stability, antigenicity, and protein expression of the severe acute respiratory syndrome coronavirus 2 spike protein trimer using structure-directed mutagenesis to alter a cavity in the core of the spike protein.
Protein folding studies have revealed that such protein core cavities can destabilize the protein, and the thermal stability can be improved by using bulkier hydrophobic residues to fill the cavity. Using this technique to improve the stability of SARS-CoV-2 spike protein antigens could elicit more stable and long-lived immune responses to vaccines.
The thermostability of the protein was assessed using differential scanning fluorimetry. Western blot analysis confirmed the expression of wild-type and mutated spike glycoprotein in transfected cells, while the membrane fusion ability of the spike glycoproteins was measured using cell-cell fusion assays. The fusion activity of the mutated spike proteins was determined through a luciferase assay.
Of the various S2P-FHA mutants produced, two mutants elicited high neutralizing antibody titers against the ancestral Wuhan-Hu-1 strain and the Delta variant. In one of the mutants , the alanine in the 1016 position was replaced with a leucine residue, while in the other mutant , the 1016 and 1020 alanine residues were replaced with valine and isoleucine, respectively. However, the neutralizing antibodies elicited by these mutants against the Omicron BA.1 subvariant were comparatively lower.
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