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. 2021 Sep 28;11:19183. doi: 10.1038/s41598-021-98707-0

Figure 2.

Figure 2

Immunoblotting with antibodies raised to PfMSA180-derived recombinant proteins detects the full-length PfMSA180 and displays processing of the protein in late schizont stages. Polyclonal antibodies raised in mice against the PfMSA180 recombinant proteins specifically detect the ~ 180 kDa protein in P. falciparum schizont lysates. WT- Wild type: schizont lysate prepared from control DMSO treated parasites, iKO- inducible knockout: schizont lysate prepared from rapamycin-treated parasites lacking MSA180 expression (see Fig. 5). Immunoblot analysis further detected additional polypeptides that may be fragments consistent with the protein undergoing proteolytic cleavage. Antibodies targeting N-terminal C1 recombinant protein identified the full-length protein (~ 180 kDa), and processed fragments of approximately 135 kDa, 100 kDa, 75 kDa and 63 kDa. C2-construct antibodies identified full-length protein (~ 180 kDa), and processed fragments of approximately 125 kDa and 96 kDa. C3-antibodies identified full-length protein (~ 180 kDa), and processed fragments of approximately 125 kDa and 75 kDa. C-terminal C4-antibodies identified full-length protein (~ 180 kDa), and processed fragments of approximately 75 kDa, 63 kDa and 48 kDa. Immunoblotting of the same parasite lysate preparation with anti-CyRPA antibodies on the same membrane was performed as loading control for late schizont stages. Full length immunoblots are shown in Supplementary Fig. 9.