Fig. 5: Profile of NiV G-specific mAbs isolated from NiV G nanoparticle-immunized mice. | npj Vaccines

Fig. 5: Profile of NiV G-specific mAbs isolated from NiV G nanoparticle-immunized mice.

From: An attachment glycoprotein nanoparticle elicits broadly neutralizing antibodies and protects against lethal Nipah virus infection

Fig. 5: Profile of NiV G-specific mAbs isolated from NiV G nanoparticle-immunized mice.The alternative text for this image may have been generated using AI.

a 27 NiV G-binding mAbs were generated from NiV G-ferritin immunized mice, and the neutralizing potency of these mAbs against NiV-M was determined using a NiV pseudovirus neutralization assay. Data shows the mean and SD from three independent experiments performed in duplicate. b The competition binding assay among isolated NiV G mAbs for binding to NiV sG protein was measured by biolayer interferometry (BLI). The 27 NiV G mAbs were grouped into four classes. The indicated mAb in the column was first loaded onto protein A biosensors; then, the biosensors were dipped into a buffer with NiV sG protein, followed by immersion into the buffer containing the second mAb. An increasing BLI signal when the addition of the second mAb indicates an unoccupied epitope (non-competitor, shown “+” in the table), whereas no binding indicates epitope blocking (competition, shown “−” in the table). HENV-26, HENV-32, and nAH1.3 are previously reported mAbs that target distinct epitopes on NiV G. The results represent two independent experiments. c Representative competition binding BLI curves of S1E2 and S2B10.

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