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. 2011 Jan 19;85(7):3095–3105. doi: 10.1128/JVI.02360-10

FIG. 9.

FIG. 9.

Multipoint mutagenesis of Bristol VP2. (A) Three-dimensional location of amino acids identified in Fig. 8 (outlined residues) on the inner surface of the core shell. Neighboring VP2 monomers in a dimeric unit (inside view) are seen in a surface representation. Point mutations of residues of the apical (api) and central (cent) subdomains are shown in blue and green, respectively. Each Bristol VP2 residue at the colored sites was changed to match the corresponding residue of SA11 VP2. (B) Purified VP2 proteins. VP2 proteins were electrophoresed in a 10% SDS-polyacrylamide gel and visualized by PageBlue staining. Molecular size markers are shown (in kilodaltons). (C) In vitro dsRNA synthesis. Reactions proceeded in the absence (none) or the presence of the different core shell proteins listed above the gel. Radiolabeled dsRNA products were resolved with 10% SDS-polyacrylamide gels and detected by autoradiography.