Table S1 (Differences in NAg sites among all unique VDPV2 NAg site amino acid replacement variants.)
Table S2 (Neutralization of VDPV2 antigenic variants by immune human sera.)
Fig. S1 (Distribution by category of the estimated nucleotide substitutions across the capsid region among all 403 2005 to 2011 Nigerian VDPV2 isolates.)
Fig. S2 (Number of independent amino acid replacements in each position of the capsid region of all 403 Nigerian VDPV2 variants isolated from 2005 to 2011.)
Fig. S3 (Replacements in NAg sites mapped onto maximum clade credibility trees of cVDPV2 lineage groups.)
Fig. S4 (Replacements in hypervariable residues 1001 to 1032 mapped onto maximum clade credibility trees of cVDPV2 lineage groups.)
Fig. S5 (Replacements in all capsid domains except NAg sites and hypervariable residues 1001 to 1032 mapped onto maximum clade credibility trees of cVDPV2 lineage groups.)
Fig. S6 (Alignment of all 25 unique VDPV2 PVR binding site variants with the reference parental Sabin 2 sequence.)
Fig. S7 (Maximum parsimony tree of all 25 unique VDPV2 PVR binding site variants and Sabin 2.)
Fig. S8 (Alignment of all 133 unique VDPV2 1001 to 1032 replacement variants with the reference parental Sabin 2 sequence.)
Fig. S9 (Maximum parsimony tree of all 133 unique VDPV2 1001 to 1032 replacement variants and Sabin 2.)
Fig. S10 (Alignment of all 120 unique VDPV2 NAg site amino acid replacement variants and MEF-1 with the reference parental Sabin 2 sequence.)
Fig. S11 (NAg sites mapped to the X-ray crystallographic structure of the poliovirus capsid pentamer.)
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