Article
wt
K378AK386AD389AN439AK444AG447RV483AF486AN487AQ493AS494AP499RT500RN501AY505A0.00.20.40.60.81.01.21.4COV2-209 4
*0.0 0100 200300 4000.51.01.52.02.5COV2-209 4Time (seconds)Response (nM)wtK378AK386AD389AN439AK444AG447RV483AF486AN487AQ493AS494AP499RT500N501RY505AA0.00.20.40.60.81.01.21.4COV2-2096Response (Normalized)*0 100 200 300 40001234COV2-209 6Time (seconds)wtK378AK386AD389AN439AK444A
G447RV483A
F486AN487AQ493AS494A
P499R
T500RN501AY505A0.00.20.40.60.81.01.21.4 COV2-213^00100 200300 4000.00.51.01.5Time (seconds)COV2-213 0wtK378AK386AD389AN439AK444A
G447RV483AF486AN487AQ493AS494AP499RT500RN501AY505A0.00.20.40.60.81.01.21.4COV2-21650 100 200 300 4000.00.51.01.52.0Time (seconds)COV2-216 5wt
K378AK386AD389AN439AK444AG447RV483AF486AN487AQ493AS494AP499RT500RN501AY505A0.00.20.40.60.81.01.21.4COV2-219 6(^00100200300400)
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COV2-219 6
Time (seconds)
Response (nM)
Response (nM)
Response (nM)
a
b
Response (Normalized
)
Response (Normalized)
Response (nM)
Response (Normalized)
Response (Normalized)
180°
K378A
K386A (^) D389A
N439A
K444A
G447R V483A
F486A
Q493A
S494A
P499R
N501A (^) T500R
Y505A
N487A
F486A
Q493A
COV2-2196 COV2-2165 COV2-2096 COV2-2130
Internal Trimer Face External Trimer Face
COV2-2094
Extended Data Fig. 5 | Mapping of critical contact residues for monoclonal
antibodies by alanine and arginine mutagenesis and biolayer interferometry.
a, Bar graphs show response values for monoclonal antibody binding to
wild-type or mutant SRBD constructs normalized to the wild type. Asterisks
denote residues where increased dissociation of monoclonal antibody was
observed, probably indicating that the residue is proximal to the monoclonal
antibody epitope. Full response curves for monoclonal antibody association
and dissociation with wild-type or mutant SRBD constructs are also shown.
b, Structure of the RBD, highlighting the critical contact residues for several
monoclonal antibodies and their location on the structure.