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. 2015 Dec 2;10(12):e0139591. doi: 10.1371/journal.pone.0139591

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© 2015 Dorin-Semblat et al

This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are properly credited.

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Fig 7 — (A) CK1 peptide phosphorylation by culture supernatants. (B) PfCK1 activity immunoprecipitated from culture supernatants of uninfected (uRBCs) or 3D7-infected (iRBC) red blood cells using an anti-PfCK1 antibody (α-PfCK1). A pre-immune serum (preim) was used as control. (C) Accumulation of casein kinase activity immunoprecipitated from supernatants of synchronised trophozoite cultures using antibodies against PfPK7, PfNek-1 and PfCK1. All three kinases immunoprecipitated from parasite extracts gave strong signals (not shown). (D) Secretion of endogenous GFP-tagged PfCK1. Anti-GFP Western blot showing GFP-tagged PfCK1 in the supernatant of transgenic parasites expressing GFP-tagged PfCK1, but not in supernatants of WT parasites. (E) Kinase activity immunoprecipitated with an anti-GFP antibody from culture supernatants. Lane 1: supernatant from a wild-type 3D7 culture; lane 2: supernatant from a transgenic line expressing GFP-tagged PfCK1.