Table 2 Binding characteristics of mutant Nipah antibodies. Binding of each Nipah antibody to the wild-type GP was determined using indirect ELISA. The data represent mean ± SD for at least two independent determinations.

From: Prediction of the binding interface between monoclonal antibody m102.4 and Nipah attachment glycoprotein using structure-guided alanine scanning and computational docking

 

Mutation

Kd (nM)

VH

WT

0.12 ± 0.002

K31A

0.08 ± 0.01

I54A

0.13 ± 0.004

L55A

0.10 ± 0.007

G56A

0.09 ± 0.01

I57A

0.10 ± 0.01

R102A

0.09 ± 0.02

E103A

1.83 ± 0.66

Q104A

0.10 ± 0.02

L105A

0.10 ± 0.006

A106W

4.95 ± 0.11

P107A

0.09 ± 0.02

H108A

0.09 ± 0.02

P109A

0.10 ± 0.02

S110A

0.13 ± 0.03

Q111A

0.08 ± 0.02

Y112A

0.11 ± 0.02

Y113A

0.12 ± 0.001

Y114A

0.07 ± 0.004

VL

R30A

0.13 ± 0.007

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