Fig. 4: Structural analysis of vaccine-elicited TCRs in complex with pMHC reveals a critical amino acid residue restricting mutation coverage. | Nature Communications

Fig. 4: Structural analysis of vaccine-elicited TCRs in complex with pMHC reveals a critical amino acid residue restricting mutation coverage.

From: Resistance potential of the HLA-A2-restricted immunodominant SARS-CoV-2-specific CD8+ T cell receptor repertoire to antigenic drift

Fig. 4: Structural analysis of vaccine-elicited TCRs in complex with pMHC reveals a critical amino acid residue restricting mutation coverage.

a Heatmap of hierarchically clustered individual TCR fingerprints (23 TCRs plotted). TCR binding strength is normalized by row. TCR communities are annotated on the left. b Pairwise Pearson correlations and hierarchical clustering of each TCR by their binding patterns. Size of the dot represents the inverse P-value. Color intensity represents the correlation coefficient. Select TCR communities are indicated. TCR clones are indicated in the vertical and diagonal axis of the plot. c Interaction of R5 (top) and T6 (bottom) residues of COV-S-082 with SVAR-14 TCRα (orange) and TCRβ (green) during MD simulations. d Same as (c), showing F7 (top) and L8 (bottom) residues. e Total contact between COV-S-082 residues and TCRα/β for 7RTR29 (top) and SVAR-14 (bottom) TCRs during simulation.

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