Figure 6
Figure 6. Surface-exposed PfEMP1 is reduced in Pf332 KO parasite lines. Western blot analysis of Triton X-100-insoluble/SDS-soluble membrane fractions from uninfected RBCs or iRBCs (3D7, 3D7ΔPf332 [11G7, 12F3, 13E2, and 13F7]), either with (+) or without (−) treatment with trypsin. The 2 bands below full-length PfEMP1 at approximately 250 kDa represent cross-reactivity with the RBC cytoskeletal proteins α and β spectrin. The approximately 80-kDa band detected after treatment with trypsin (VARC) represents the cytoplasmic domain of surface-exposed PfEMP1 in these iRBCs. An identical blot was probed for HSP70 as a parasite-loading control and with anti–glycophorin C (GpC) as a control for digestion of RBC surface proteins.

Surface-exposed PfEMP1 is reduced in Pf332 KO parasite lines. Western blot analysis of Triton X-100-insoluble/SDS-soluble membrane fractions from uninfected RBCs or iRBCs (3D7, 3D7ΔPf332 [11G7, 12F3, 13E2, and 13F7]), either with (+) or without (−) treatment with trypsin. The 2 bands below full-length PfEMP1 at approximately 250 kDa represent cross-reactivity with the RBC cytoskeletal proteins α and β spectrin. The approximately 80-kDa band detected after treatment with trypsin (VARC) represents the cytoplasmic domain of surface-exposed PfEMP1 in these iRBCs. An identical blot was probed for HSP70 as a parasite-loading control and with anti–glycophorin C (GpC) as a control for digestion of RBC surface proteins.

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