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- W3154350044 abstract "The Plasmodium falciparum chloroquine resistance transporter (PfCRT) is a phospho-protein with three identified phosphorylation sites (Ser 33 , Ser 411 and Thr 416 ) at its cytosolic N- and C-termini. In this study, we report on the characterization of PfCRT anti-serum and show the presence of three epitope-specific immunoglobulin (IgG) pools ( i.e. , IgG-P1, P2, and P3), each recognizing a different epitope in PfCRT cytoplasmic C-terminal. IgG-P2 bound the heptapeptide sequence ( 408 NEDSEGE 414 ), including Ser 411 . The effect of Ser 411 phosphorylation on the binding specificity of IgG-P2 was confirmed using heptapeptides and full-length PfCRT with substitutions of Ser 411 with aspartic acid (phospho-serine mimic) and alanine residues. Moreover, using purified IgG-P2, we show the presence of PfCRT homodimer that has un-phosphorylated Ser 411 and migrates with an apparent molecular mass of 90 kDa on SDS-PAGE. In addition, parasite lysates showed PfCRT to be more phosphorylated at Ser 411 in CQ-sensitive (3D7) than CQ–resistant (Dd2-H) strains of P. falciparum . Taken together, the findings of this study suggest a role for Ser 411 phosphorylation in PfCRT structure-function. • High resolution mapping of anti-PfCRT antisera to its C-terminal sequence. • Isolation of three reactive IgG pools in PfCRT antisera against different epitopes, with IgG pool 2 specific to Ser 411 phosphorylation status. • Demonstrating the presence of PfCRT homodimer, ∼90 kDa, encoding un-phosphorylated Ser 411 . • PfCRT phosphorylation status at Ser 411 may predict P. falciparum resistance to chloroquin." @default.
- W3154350044 created "2021-04-26" @default.
- W3154350044 creator A5054250393 @default.
- W3154350044 creator A5070128366 @default.
- W3154350044 date "2021-06-01" @default.
- W3154350044 modified "2023-09-24" @default.
- W3154350044 title "Epitope-specific IgG pools identify PfCRT monomer and homodimer polypeptides that are differentially phosphorylated at Ser411 in Plasmodium falciparum" @default.
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- W3154350044 doi "https://doi.org/10.1016/j.bbrc.2021.04.034" @default.
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