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. 2009 Feb 22;16(3):265–273. doi: 10.1038/nsmb.1566

Figure 1. In vitro binding and neutralization of anti-H5 antibodies.

Figure 1

(a) The ten antibodies were converted to soluble scFv-Fcs (scFv linked to the hinge, CH2 and CH3 domains of human IgG1) and evaluated for binding to trimeric H5-TH04 or monomeric HA1 of H5-TH04 coated on an ELISA plate. The H5 scFv-Fcs recognize trimeric H5 but not HA1. An antibody raised against HA1 (2A) recognized both. (b) Neutralization of H5-TH04–pseudotyped viruses (virus-like particles with HIV-1 only cores that display H5 on their surface). Percentage of neutralization at two concentrations is shown with s.d. The mAb 80R18 was used as a negative control (Ctrl.). (c,d) Neutralization of wild-type H5-VN04 and H5-IN05 by the ten scFv-Fcs at three concentrations using a plaque reduction assay. Results are consistent with those obtained from a microneutralization assay (data not shown).