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Mast cell‐mediated immune responses through IgE antibody and Toll‐like receptor 4 by malarial peroxiredoxin

In this study, 2‐Cys Plasmodium berghei ANKA (PbA) peroxiredoxin (Prx) was identified as an antigenic protein recognized by an anti‐PbA IgE antibody using two‐dimensional polyacrylamide gel electrophoresis and proteomic analysis. Innate immune responses to PbAPrx were examined using cells from mice deficient in Toll‐like receptors (TLR) or related molecules, and it was demonstrated that responses were severely impaired in TLR4–/–, MyD88–/– and MD‐2–/– mice, but not in Toll/IL‐1 receptor domain‐containing adaptor inducing IFN‐γ (TRIF)–/–, TLR2–/– or radioprotective 105 (RP105)–/– mice. An association between PbAPrx and TLR4 was observed following immunoprecipitation and immunoblotting, suggesting that PbAPrx was associated with TLR4/MD‐2. Interactions between Prx and TLR4/MD‐2 were also examined by flow cytometry using TLR4/MD‐2‐ or TLR2‐expressing cells. NFκB/GFP activity was observed in TLR4/MD‐2‐ but not in TLR2‐expressing cells following stimulation with Prx. However, this effect was not observed after treatment with proteinase K, suggesting that PbAPrx is a protein ligand for TLR4 and that the PbAPrx activity observed in this study is not due to contamination with LPS. These findings indicate that malarial Prx induces IgE‐mediated protection through FcϵRI on mast cells and innate immunity through TLR4 with MyD88 and MD‐2, suggesting a novel function for malarial Prx in innate and acquired immune responses in malaria.