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. 2012 Sep 4;287(44):37219–37232. doi: 10.1074/jbc.M112.395921

FIGURE 2.

FIGURE 2.

Functional epitope of mAb PRC7. A, Western blot reactivity with various PrP primary structures. Samples from hamsters, mink, ferret, and squirrel monkey were prion infected. Syr., Syrian; Chin., Chinese; and Arm., Armenian hamsters; Sq. Mon., squirrel monkey. B, primary structures are aligned between mouse PrP residues 152 and 198. Reactive species are boxed and shaded red. Glycans attached at residues 180 and 196 are shown as green hexagons. Residues 154 and 185 are boxed and shaded blue, and side chains are yellow in the tertiary structure. C, Western blots of RK13 cell extracts transfected with the following: Mo N154, mouse PrP with Asn at residue 154; Mo E185, mouse PrP with Glu at residue 185; Mo N154/E185, mouse PrP with Asn at residue 154 and Glu at residue 185; SHa wt, wild type Syrian hamster PrP; SHa Y155, Syrian hamster PrP with Tyr at residue 155; Bo wt, wild type cattle PrP; Bo Y166, cattle PrP with Tyr at residue 166; Bo Y166/Q197, cattle PrP with Tyr at residue 166, and Gln at residue 197.