Structural evidence for the critical role of the prion protein hydrophobic region in forming an infectious prion
Fig 3
Nb484 interacting with the hydrophobic region of PrPC.
(A) Influence of Nb484 on the interaction of PrP and POPG synthetic lipid. For rPrP+POPG+Nb484, recombinant mouse PrP was incubated with POPG before mixed with Nb484 at different molar ratios (Nb484:recPrP = 0, 1, 2, 4, or 8:1). For rPrP+Nb484+POPG, recombinant mouse PrP was incubated with Nb484 at different molar ratios (Nb484:recPrP = 0, 1, 2, 4, or 8:1) before mixed with POPG. PK-resistant PrP was detected using POM1 antibody. (B) Representative ELISA results show that both Nb484 and Nb862 bind strongly to rPrP. Nb484 has very week binding to ΔHC, but Nb862 shows strong binding signal to ΔHC. POM1 antibody was used as a primary antibody to determine the binding signal. POM1 displayed similar binding for both rPrP and ΔHC. All results are the average of 3 replicates.rPrP: MoPrP(23–230), ΔHC: MoPrPΔHC.