Bailey, Adam L

Case, James Brett

Chen, Rita E

Dejnirattisai, Wanwisa

Diamond, Michael S

et al.,

Kafai, Natasha M

Ying, Baoling

English

Digital Commons@Becker

Cell, Volume 184Supplemental informationThe antigenic anatomy of SARS-CoV-2receptor binding domainWanwisa Dejnirattisai, Daming Zhou, Helen M. Ginn, Helen M.E. Duyvesteyn, PiyadaSupasa, James Brett Case, Yuguang Zhao, Thomas S. Walter, Alexander J.Mentzer, Chang Liu, Beibei Wang, Guido C. Paesen, Jose Slon-Campos, César López-Camacho, Natasha M. Kafai, Adam L. Bailey, Rita E. Chen, Baoling Ying, CraigThompson, Jai Bolton, Alex Fyfe, Sunetra Gupta, Tiong Kit Tan, Javier Gilbert-Jaramillo, William James, Michael Knight, Miles W. Carroll, Donal Skelly, ChristinaDold, Yanchun Peng, Robert Levin, Tao Dong, Andrew J. Pollard, Julian C. Knight, PaulKlenerman, Nigel Temperton, David R. Hall, Mark A. Williams, Neil G. Paterson, FelicityK.R. Bertram, C. Alistair Siebert, Daniel K. Clare, Andrew Howe, Julika Radecke, YunSong, Alain R. Townsend, Kuan-Ying A. Huang, Elizabeth E. Fry, JuthathipMongkolsapaya,Michael S. Diamond, Jingshan Ren, David I. Stuart, andGavin R. ScreatonParticipantsFemale 16Male 26Average Age (y) 55.4 (IQR 47-61)Days post-symptom onset 45.5 (IQR 40-53)Disease severityAsymptomatic 1 (2.4%)Mild 28 (66.6%)Severe 12 (28.6%)Critical 1 (2.4%)Table S1. Summary of SARS-CoV-2-infected patients enrolled in the study, related to STAR Methods, Patient and blood samples.Table S2. Neutralisation IC50 and biolayer interferometry (BLI) measurements of affinity (KD) and on (Ka) and off (Kdis) rates for selected mAbs (except for 159 BLI measurements are for Fabs). Related to STAR Methods Focus Reduction Neutralization Assay (FRNT) and Competition assay of antibodies.IgG Neutralization IC50 (ug/ml)#KD (nM) $Ka (1/Ms)  $Kdis (1/s) $45 2.005* 5.9 7.8E04 4.6E-0455 0.037 ± 0.008 3.6 1.1E05 3.9E-0458 0.046  ± 0.016 3.4 1.0E05 3.6E-04132 0.054  ± 0.014 3.1 1.1E05 3.3E-04148 6.734* 4.0 7.6E04 3.0E-04150 0.023  ± 0.003 0.9 2.1E05 1.9E-04158 0.034  ± 0.003 0.7 1.2E05 8.4E-05165 0.021  ± 0.006 4.8 7.0E04 3.3E-04170 0.025* 2.7 1.7E05 4.5E-04175 0.033  ± 0.009 2.4 2.8E05 6.5E-04222 0.016  ± 0.003 3.0 1.2E05 3.5E-04253 0.040  ± 0.007 4.5 1.4E05 6.1E-04253H55L 0.004  ± 0.000 1.5 3.0E05 4.5E-04253H165L 0.003  ± 0.000 3.1 1.2E05 3.9E-04269 0.036  ± 0.009 2.2 1.8E05 3.9E-04278 0.009  ± 0.002 3.0 2.6E05 7.8E-04281 0.005  ± 0.001 1.0 2.3E05 2.3E-04282 0.073  ± 0.009 1.5 1.6E05 2.4E-04316 0.010  ± 0.002 2.0 3.5E05 7.1E-04318 0.015  ± 0.002 7.6 6.7E04 5.1E-04384 0.002  ± 0.001 2.7 1.1E05 2.9E-04159 (anti-spike) 0.005  ± 0.001 1.1 5.7E05 6.3E-04# Neutralization activity of selected antibodies against SARS-CoV-2 were determined by FRNT. Data are from 3 independent experiments, each with duplicate wells and the data are shown as mean ± s.e.m.*FRNT was performed once with duplicate wells.$ Determined for Fab fragmentsmax 20% competition<0.1 ug/ml IC5055  58 55 278 58  88 58 132 58 150 58 158 58 165 58 175 58 222 58 282 88 278 132 278 150 278 158 278 165 278 175 278 222 278 278 282 Table S3. Antibody coordinates, epitope assignment and IC50 values for the 80 RBD binders and pairs and triplets of non-competing antibodies from cluster analysis. Related to STAR Methods Competition mapping of antibodies.Coordinates in pseudo-water ‘PDB’ format: residue_ID=Ab_number, chain_ID=epitope, Occupancy=RMSD from Monte Carlo, B=Log(IC50[uM]) max 20% competition<1 ug/ml IC5040 318 40 334 40 382 55  58  61 55  61 278 55  61 318 55  61 334 55  61 361 55  61 382 58  61 165 58  61 175 58  88 58 132 58 150 58 158 58 222 58 282 61 165 278 61 165 318 61 165 334 61 165 361 61 165 382 61 170 334 61 175 278 61 175 318 61 175 334 61 175 361 61 175 382 61 181 334 61 182 334 61 183 334 61 281 334 61 316 334 61 334 384 61 334 394 61 334 398 88 278 88 318 88 334 88 361 88 382 132 278 132 318 132 334 132 361 132 382 150 278 150 318 150 334 150 361 150 382 158 278 158 318 158 334 ATOM      1  AB  HOH Z   1     219.988 209.996 175.029  7.43  2.00         ATOM      2  AB  HOH W   2     241.900 217.482 139.154  8.51  2.00         ATOM     22  AB  HOH Z  22     217.812 203.466 170.490  4.98  2.00         ATOM     38  AB  HOH Z  38     219.118 209.290 156.724 12.77  2.00         ATOM     40  AB  HOH V  40     227.132 202.980 138.890  0.00 -1.32         ATOM     45  AB  HOH Y  45     243.041 201.662 165.392  5.90  0.92         ATOM     51  AB  HOH Y  51     240.512 213.630 174.143 11.83  0.33         ATOM     54  AB  HOH Z  54     224.162 216.829 178.651 10.51  2.00        ATOM     55  AB  HOH V  55     230.392 202.791 136.613  6.47 -1.42        ATOM     57  AB  HOH Y  57     244.237 208.839 171.111 17.86  0.25         ATOM     58  AB  HOH X  58     248.948 211.008 154.261  3.28 -1.64         ATOM     61  AB  HOH Z  61     215.370 201.510 158.862  9.19 -0.31         ATOM     75  AB  HOH X  75     249.472 209.361 144.241  4.43  0.47         ATOM     78  AB  HOH Y  78     243.439 212.348 167.679  8.02  2.00        ATOM     79  AB  HOH Y  79     240.144 214.276 175.407  9.89  0.64        ATOM     88  AB  HOH V  88     226.831 203.596 139.701  8.02 -1.51        ATOM     91  AB  HOH Y  91     243.785 214.036 163.803  5.44  0.45        ATOM    120  AB  HOH Y 120     241.052 215.135 166.628  8.48  2.00        ATOM    132  AB  HOH V 132     225.151 203.146 140.780  7.34 -1.51         ATOM    140  AB  HOH Z 140     218.037 201.529 170.470  7.17  2.00         ATOM    143  AB  HOH Y 143     241.246 212.069 173.138 12.67  0.36         ATOM    144  AB  HOH Y 144     239.212 219.880 163.947  9.32  0.53         ATOM    150  AB  HOH V 150     225.177 199.643 138.903  6.21 -1.47         ATOM    155  AB  HOH Z 155     218.779 195.978 165.617 10.90  0.88        ATOM    158  AB  HOH V 158     225.142 200.374 139.122  6.14 -1.19        ATOM    163  AB  HOH Z 163     216.360 203.294 166.704  7.82  0.91        ATOM    164  AB  HOH X 164     240.165 218.613 161.087  5.45  2.00        ATOM    165  AB  HOH V 165     229.346 202.859 137.309  8.73 -1.74         ATOM    170  AB  HOH W 170     237.903 207.543 138.527 18.08 -0.32         ATOM    172  AB  HOH Y 172     236.338 222.258 160.965  8.11  0.69         ATOM    175  AB  HOH V 175     226.262 210.195 144.027 14.62 -1.66         ATOM    177  AB  HOH Z 177     219.823 202.734 173.330  7.86  0.95         ATOM    178  AB  HOH Z 178     217.146 205.246 158.026 11.23  0.46         ATOM    181  AB  HOH W 181     237.022 211.814 140.007  8.31 -0.48         ATOM    182  AB  HOH W 182     237.022 211.814 140.007  9.40 -0.68         ATOM    183  AB  HOH W 183     234.883 216.679 140.697 11.84 -0.26         ATOM    185  AB  HOH Y 185     240.359 217.188 164.380 10.53  2.00         ATOM    187  AB  HOH W 187     236.113 215.662 140.482  9.30  0.29         ATOM    189  AB  HOH Z 189     216.091 202.041 165.781 13.13  2.00         ATOM    217  AB  HOH Y 217     241.885 215.173 164.589  6.05  0.85         ATOM    219  AB  HOH V 219     231.498 192.382 152.478 25.53 -0.45         ATOM    222  AB  HOH V 222     223.317 201.424 142.277 10.62 -1.66         ATOM    238  AB  HOH W 238     235.903 214.120 140.733 13.95 13.95         ATOM    242  AB  HOH W 242     239.488 211.308 138.735  7.00  7.00         ATOM    253  AB  HOH V 253     229.489 200.810 134.904 11.11 -1.28         ATOM    263  AB  HOH W 263     242.805 196.670 145.565  6.74  2.00         ATOM    264  AB  HOH W 264     243.377 207.940 138.866 13.12  2.00         ATOM    269  AB  HOH V 269     223.332 201.991 142.481  9.72 -1.28         ATOM    270  AB  HOH W 270     242.360 195.917 146.938  9.16  1.00         ATOM    273  AB  HOH Z 273     220.567 195.229 167.847  7.59  2.00         ATOM    278  AB  HOH X 278     250.677 207.639 147.773  4.81 -1.23         ATOM    280  AB  HOH Z 280     220.096 200.424 173.531  7.78  1.00         ATOM    281  AB  HOH W 281     243.808 202.220 141.718 12.48 -2.22         ATOM    282  AB  HOH V 282     224.323 198.309 139.537  4.46 -1.47         ATOM    292  AB  HOH Y 292     244.625 207.249 171.203  9.89  0.68         ATOM    293  AB  HOH Y 293     241.351 215.759 163.963  7.17  2.00         ATOM    300  AB  HOH V 300     228.706 214.209 143.978 16.87  2.00         ATOM    301  AB  HOH V 301     223.057 205.429 145.036 16.69  2.00         ATOM    314  AB  HOH Z 314     220.665 209.331 165.719  9.16  2.00         ATOM    315  AB  HOH X 315     250.105 211.317 149.429  3.55  0.27         ATOM    316  AB  HOH W 316     236.386 202.405 135.598 13.71 -1.72         ATOM    318  AB  HOH X 318     251.029 206.311 152.504  4.57 -0.33         ATOM    334  AB  HOH Y 334     231.527 218.600 158.544 15.81 -0.24         ATOM    336  AB  HOH Y 336     243.656 201.501 170.761  8.98  2.00         ATOM    337  AB  HOH X 337     246.808 214.372 157.360  7.31  2.00         ATOM    340  AB  HOH Z 340     218.843 197.397 169.870 11.79  2.00         ATOM    361  AB  HOH X 361     250.487 206.197 150.651  5.41 -0.09         ATOM    369  AB  HOH Y 369     243.446 201.373 166.570 14.97  0.01         ATOM    373  AB  HOH Z 373     230.940 192.660 163.268  9.00  2.00         ATOM    379  AB  HOH X 379     246.540 202.168 150.446  9.74  1.00         ATOM    382  AB  HOH X 382     246.528 202.685 156.748  4.09 -0.20         ATOM    384  AB  HOH W 384     240.568 201.666 137.825  8.34 -2.40         ATOM    386  AB  HOH X 386     243.678 201.814 160.033  6.14  2.00         ATOM    387  AB  HOH Y 387     242.323 201.191 165.021 10.29  2.00         ATOM    393  AB  HOH Z 393     229.130 191.944 161.721  9.73  2.00         ATOM    394  AB  HOH W 394     242.360 195.917 146.938 16.59 -1.77         ATOM    398  AB  HOH W 398     239.534 192.608 143.991 13.34 -1.07         ATOM    400  AB  HOH Y 400     242.184 200.410 166.818 13.16  2.00         ATOM    411  AB  HOH W 411     231.577 214.255 143.535 16.41  0.03         ATOM    412  AB  HOH W 412     235.358 213.955 140.720 16.23  1.00 Thermofluor (reporter dye) DLS @ 20 CFraction soluble after N freeze-thaw cyclesAntibody id Tm 1Propnof melt Tm 2Propnof meltPeak1 MWPeak1 %mass N=5 N=202 78.4 146.25 10022 80.7 177.55 99.9840 73.8 215.20 100.00 0.9 0.844 77.6 0.9 89.1 0.1 685.57* 100.0045 75.9 0.3 86.6 0.8 146.17 100.00 1.0 0.854 71.9 0.9 87.2 0.1 177.31 99.7155 75.9 0.4 86.7 0.7 215.20 99.83 1.0 0.958 80.6 213.93 99.98 0.9 0.961 75.9 0.9 87.1 0.1 146.17 100.0075 75.3 0.4 84.1 0.7 215.08 100.00 0.9 1.088 73.3 213.93 100.00 1.0 0.9111 80.1 214.23 100.00132 69.1 0.7 79.7 0.3 146.25 99.96 1.0 0.6140 79.0 260.07 99.90148 75.4 0.3 85.4 0.7 213.93 99.98150 71.1 0.9 89.1 0.1 176.08 100.00 1.0 0.7158 76.4 0.9 88.4 0.1 213.93 99.91 1.0 0.9165 78.2 177.31 100.00 1.0 1.0170 64.9 0.8 76.1 0.2Out of Range 99.16 0.9 1.0175 74.3 215.08 100.00 1.0 0.9177 74.3 176.08 99.93222 76.7 214.05 100.00 0.9 0.9253 75.9 146.17 100.00 1.0 0.9269 73.7 214.90 100.00 0.9 0.8278 76.2 1.0 88.0 0.1 316.65 100.00 1.0 0.8281 70.5 214.23 100.00 0.9 0.8282 70.8 0.9 88.3 0.1 215.08 99.99 0.9 0.9316 74.9 465.66 100.00 0.9 0.9318 72.1 0.9 86.7 0.1 144.84 100.00384 74.9 0.9 88.0 0.1 146.17 100.00 1.0 0.8253H165L 74.5 0.6 86.4 0.4 176.08 100.00 0.9 0.7253H55L 74.2 0.6 87.3 0.4 175.84 100.00 0.9 0.9Table S4. Stability tests for selected antibodies using thermofluorand dynamic light scattering (DLS). Related to STAR Methods Physical assays.Table S5. X-ray data collection and refinement statistics (molecular replacement). Related to STAR Methods X-ray data collection, structure determination and refinement. Structure RBD-88-45  RBD-150  RBD-158 (form 1) RBD-158 (form 2) RBD-253-75  RBD-253H55L-75  RBD-scFV269  RBD-316 RBD-384-S309 PDB ID 7BEL 7BEI 7BEJ 7BEK 7BEN 7BEO 7BEM 7BEH 7BEP Data collection          Space group C2a  C2221 C2221 C2221 P212121a P21 P6222 P21212 P212121 Cell dimensions                a, b, c (Å) 180.1, 140.7, 131.0 81.4, 150.7, 145.5 53.2, 232.3, 135.2 83.0, 149.4, 145.5 93.2, 149.8, 229.1 93.4, 150.1, 116.1 173.6, 173.6, 120.6 104.0, 150.9, 46.0 108.8, 113.2, 302.8     a, b, g (°)  90, 124.6, 90 90, 90, 90 90, 90, 90 90, 90, 90 90, 90, 90 90, 92.0, 90 90, 90, 120 90, 90, 90 90, 90, 90 Resolution (Å) 59–2.53 (2.57–2.53)b  52–2.30 (2.34–2.30) 53–2.42 (2.46–2.42) 51–2.04 (2.08–2.04) 59–2.50 (2.54–2.50) 66–3.19 (3.25–3.19) 57–2.52 (2.56–2.52) 52–2.30 (2.34–2.30) 63–2.61 (2.65–2.61) R merge 0.189 (---) 0.192 (0.990) 0.250 (---) 0.118 (---) 0.283 (---) 0.412 (---) 0.432 (---) 0.107 (---) 0.112 (---) R pim 0.079 (1.101) 0.039 (0.362) 0.051 (0.781) 0.033 (1.296) 0.056 (1.526) 0.169 (1.189) 0.051 (2.921) 0.032 (1.042) 0.032 (0.982) I/s(I) 5.6 (0.3) 12.5 (0.5) 7.6 (0.4) 13.1 (0.5) 7.3 (0.3) 4.0 (0.5) 9.2 (0.2) 14.2 (0.6) 13.1 (0.5) CC1/2 0.995 (0.326) 0.997 (0.651) 0.993 (0.363) 0.999 (0.345) 0.999 (0.623) 0.977 (0.280) 0.999 (0.627) 0.998 (0.223) 0.998 (0.344) Completeness (%) 97.8 (75.6) 84.4 (42.8) 98.5 (85.2) 99.9 (97.2) 100 (99.5) 100 (99.5) 99.9 (96.3) 85.7 (40.2) 100 (99.1) Redundancy 6.6 (5.0) 22.0 (8.2) 23.7 (13.5) 13.4 (9.9) 26.6 (24.8) 6.9 (7.1) 73.4 (54.1) 11.0 (4.9) 13.3 (12.3)           Refinement          Resolution (Å) 49–2.53 43–2.30 53–2.42 43–2.04 58–2.50 58–3.19 47–2.52 45–2.30 63–2.61 No. reflections 81142/4196 30799/1567 30107/1610 54733/2897 105179/5570 50411/2657 33910/1753 26846/1392 108562/5577 R work / Rfree 0.250/0.285 0.197/0.236 0.195/0.229 0.200/0.220 0.242/0.284 0.232/0.274 0.217/0.248 0.218/0.233 0.206/0.241 No. atoms              Protein 13221 4787 4777 4816 16052 16152 3235 4768 16682     Ligand/ion 158 47 68 98 187 177 47 104 234 B factors (Å2 )              Protein 70 49 58 63 73 90 91 60 98     Ligand/ion 86 84 82 91 97 114 139 74 124 r.m.s. deviations              Bond lengths (Å) 0.003 0.005 0.003 0.002 0.002 0.002 0.003 0.002 0.003     Bond angles (°) 0.7 0.8 0.6 0.6 0.6 0.5 0.6 0.5 0.6 aPresence of translational NCS.  bValues in parentheses are for highest-resolution shell.      Table S6. Cryo-EM data collection, refinement and validation statistics for Spike/Fab(IgG) complexes. Related to STAR Methods Cryo-EM Data collection and processing.Cryo-EM data collection, refinement and validation statistics of spike/COVOX-Fab complexes Complex (EMD ID, PDB ID) 40 (EMD-12274, 7ND3) 88 (EMD-12275, 7ND4) 150 (EMD-12276, 7ND5) 158* (EMD-12277, 7ND6) 316 (EMD-12278, 7ND7) 384 (EMD-12279, 7ND8) 253H55L (EMD-12280, 7ND9) 253H55L (EMD-12281, 7NDA) 253H165L (EMD-12282, 7NDB) 159 (EMD-12283, 7NDC) 159 (EMD-12284, 7NDD) Data collection and processing            Voltage (kV) 300   Electron exposure (e– /Å2 ) 43.1 57.6 48.8 45.3 46.0 47.7 47.2 47.2 44.7 50.5 50.5 Defocus range (μm) -0.8 to -2.6   Pixel size [super res] (Å) 0.83 [0.415] 0.82 0.82 0.82 0.82 0.82 0.83 [0.415] 0.83 [0.415] 0.83 [0.415] 0.82 0.82 Symmetry imposed C1 C3 C1 C1 C3 C1 C1 C1 C1 C3 C1 Particles in final reconstruction (no.) 39186 56686 93555 18768 162,905 73,158 206,548 47,242 31,477 13638 27880 Map resolution (Å) 3.7 3.1 3.4 6.8 3.6 3.5 2.8 3.3 4.6 4.1 4.2     FSC threshold 0.143 0.143 0.143 0.143 0.143 0.143 0.143 0.143 0.143 0.143 0.143             Refinement            Initial model used  PDB 6Z97 PDB 6ZDH PDB 6Z97 PDB 6Z97 PDB 7NDA PDB 7NDA PDB 6Z97 PDB 6VXX PDB 6Z97 PDB 7NDA PDB 7ND5 RBD conformation One-up All-up One-up One-up All-down All-down One-up All-down One-up All-down One-up Model resolution (Masked) (Å) 3.8 3.2 3.5 7.6 3.8 3.8 3.0 3.5 4.9 4.2 4.2     FSC threshold 0.5 0.5 0.5 0.5 0.5 0.5 0.5 0.5 0.5 0.5 0.5 Map sharpening B factor (Å2 ) -83 -56 -45 -369 -90 -48 -61 -37 -133 -61 -49 Model composition                Non-hydrogen atoms 25050 29848 26710 25152 29591 27659 27336 27729 27184 30648 30645     Protein residues 3194 3727 3406 26742 3699 3447 3482 3452 3460 3852 3852     Ligands 49 71 49 49 64 60 50 63 49 54 54 B factors (Å2 )                Protein 136 78 110 396 87 147 82 126 264 184 239     Ligand 135 89 96 402 104 149 94 137 258 169 183 R.m.s. deviations                Bond lengths (Å) 0.002 0.003 0.002 0.003 0.003 0.004 0.002 0.003 0.002 0.002 0.003     Bond angles (°) 0.5 0.6 0.5 0.6 0.6 0.7 0.5 0.6 0.5 0.5 0.6             Validation            MolProbity score 1.40 1.47 1.45 1.43 1.41 1.44 1.56 1.61 1.58 1.44 1.54 Clashscore 3.47 3.79 4.18 3.98 3.57 4.05 4.31 5.27 4.93 3.82 4.67 Poor rotamers (%) 0.64 0.28 0.32 0.53 0.38 0.30 0.62 0.30 0.72 0.37 0.40 Ramachandran plot                Favored (%) 96.2 95.6 96.3 96.4 96.2 96.3 94.9 95.3 95.3 96.0 95.7     Allowed (%) 3.7 4.1 3.7 3.6 3.2 3.5 4.9 4.4 4.5 4.0 4.1     Disallowed (%) 0.1 0.3 0 0 0.2 0.2 0.2 0.3 0.2 0 0.2 *, Rigid body refinement only.   Antibody Binding KD (nM) Neutralization IC50 (nM) %Occupancy40 IgG 0.33 ± 0.04 0.16 ± 0.03 33.3 ± 1.340 Fab 1.23 ± 0.19 45.68 ± 7.15 97.4 ± 0.088 IgG 0.25 ± 0.01 0.07 ± 0.04 21.9 ± 9.588 Fab 1.21 ± 0.14 6.95 ± 0.07 85.2 ± 1.6150 IgG 0.24 ± 0.01 0.08 ± 0.02 25.1 ± 5.7150 Fab 0.75 ± 0.10 0.61 ±0.23 43.2 ± 6.6158 IgG 0.50 ± 0.02 0.13 ± 0.02 20.5 ± 2.6158 Fab 3.73 ± 0.56 4.12 ± 0.04 52.7 ± 3.5159 IgG 0.19 ± 0.02 0.08 ± 0.01 30.0 ± 5.2159 Fab 0.29 ± 0.02 N/A N/A253 IgG 0.17 ± 0.01 0.36 ± 0.02 67.9 ± 2.3253 Fab 23.38 ± 3.84 N/A N/A253H55L IgG 0.09 ± 0.01 0.02 ± 0.00 19.6 ± 2.1253H55L Fab 10.19 ± 0.56 5.08 ± 0.47 33.2 ± 0.8253H165L IgG 0.09 ± 0.01 0.03 ± 0.00 24.5 ± 0.6253H165L Fab 5.02 ± 1.40 5.22 ± 1.18 51.3 ± 1.4316 IgG 0.13 ± 0.00 0.08 ± 0.02 35.4 ± 6.0316 Fab 8.76 ± 0.64 27.64 ± 9.47 74.0 ± 8.1384 IgG 0.10 ± 0.03 0.01 ± 0.00 12.1 ± 2.3384 Fab 7.86 ± 0.96 4.86 ± 0.16 38.4 ± 3.7Table S7. Affinity (KD), neutralization potency (IC50) and % occupancy against SARS-CoV-2 of full-length IgG and Fab for ten selected antibodies were determined. Related to STAR Methods Focus Reduction Neutralization Assay (FRNT) and Competition assay of antibodies.Data are from 2 independent experiments, each with duplicate wells and the data are shown as mean ± s.e.m. .  

The antigenic anatomy of SARS-CoV-2 receptor binding domain

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The antigenic anatomy of SARS-CoV-2 receptor binding domain

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