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. 2021 Aug 10;297(3):101065. doi: 10.1016/j.jbc.2021.101065

Table 1.

Summary of SPR affinity measurements

Epitope Sequence NR1C
NR2F
NR1A
NR1D
KD (μΜ) 95% CI
S269–277 YLQPRTFLL 2.71 2.75 2.36 3.72
2.30–3.18 2.21–3.40 1.92–2.89 3.33–4.15
S269–277P272L YLQLRTFLL 272.4 170.2 157.5 163.1
235.5–320.5 160.1–181.5 140.9–178.0 155.4–171.3
S269–277R273S YLQPSTFLL N.B. N.B. N.B. N.B.
S269–277T274I YLQPRIFLL 109.3 360.3 ND ND
104.2–114.7 270.6–520.8
PNRL YLQQRTFLL 77.6 5.87 ND ND
74.9–80.6 5.17–6.67
BTRL YLKPRTFML >100 >100 ND ND
SARS YLKPTTFML N.B. N.B. ND ND
MERS KQLPLTFLL N.B. N.B. ND ND
PAR1 TLDPRSFLL N.B. N.B. ND ND

TCR binding to immobilized HLA-A2S269–277 and homologous epitopes (sequence differences to the SARS-CoV-2 epitope are highlighted in bold) were measured in two independent experiments with two replicates. Dissociation constant (KD) (in bold) and confidence interval (95% CI) (in italics) were calculated from all data using a single-site-binding model with KD as a shared variable.

Abbreviations: N.B., no binding; ND, not determined.