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. 2013 May;27(5):2055–2065. doi: 10.1096/fj.12-219964

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This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/3.0/us/) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.

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Figure 6. — Mutational analysis of the RV glycoprotein using the E. coli-derived 62-71-3 scFv and the plant-derived 62-71-3 IgG. A) Phage-displayed 62-71-3 scFv was tested against a set of pseudotype viruses containing either the CVS11 wild-type glycoprotein (CVS control) or mutated CVS11 glycoproteins containing the antigenic sites of LBV (LBV site I/II/III/IV) within the CVS backbone. B) Plant-derived mAbs 62-71-3 and E559 and a nonspecific mAb were tested regarding their neutralization of pseudotype viruses containing either the CVS11 wild-type glycoprotein or a mutated CVS11 glycoprotein containing LBV antigenic site I (aa 226–231). C) Role of antigenic site I residue K226 was investigated by testing the plant-derived mAbs 62-71-3 and E559 regarding their neutralization of pseudotypes containing glycoproteins with a K226R mutation. Controls included pseudotypes containing the CVS11 wild-type glycoprotein (CVS control) or containing the CVS glycoprotein containing a nonspecific mutation within antigenic site III (N336S control). D) Neutralization of a site I mutant containing a G229E mutation by mAbs 62-71-3 and E559.