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Antigen B from Echinococcus granulosus is a novel ligand for C‐reactive protein
Author(s) -
SilvaÁlvarez Valeria,
Ramos Ana Lía,
Folle Ana Maite,
Lagos Sofía,
Dee Valerie M.,
Ferreira Ana M.
Publication year - 2018
Publication title -
parasite immunology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.795
H-Index - 75
eISSN - 1365-3024
pISSN - 0141-9838
DOI - 10.1111/pim.12575
Subject(s) - echinococcus granulosus , biology , phosphocholine , immunology , antigen , c reactive protein , phosphatidylcholine , macrophage , cytokine , interleukin 4 , microbiology and biotechnology , inflammation , biochemistry , in vitro , phospholipid , zoology , membrane
Summary Antigen B (EgAgB) is a phosphatidylcholine ( PC )‐rich lipoprotein of Echinococcus granulosus s.l. larva, potentially capable of modulating the activation of various myeloid cells, including macrophages. As C‐reactive protein ( CRP ) can act as an innate receptor with ability to bind the phosphocholine moiety of PC in lipoproteins, we investigated whether EgAgB and CRP could interact during cystic echinococcosis infection ( CE ), and how CRP binding could affect the modulation activities exerted by EgAgB on macrophages. To that end, we firstly investigated the occurrence of CRP induction during human CE . We found that 61% of CE patients, but none of healthy donors, exhibited serum CRP levels higher than 10 mg/ mL , suggesting that CRP can be induced during the chronic phase of CE . Furthermore, human CRP was capable of binding specifically to EgAgB with high affinity (0.6 ± 0.1 nM ); this binding was Ca 2+ ‐dependent and involved the phosphocholine moiety of PC , but not EgAgB8/1, EgAgB8/2 or EgAgB8/3 apolipoproteins. Finally, CRP presence altered the modulation exerted by EgAgB on the cytokine response of LPS ‐activated macrophages. Overall, our results suggest that CRP presence during CE may contribute to a complex scenario of interactions between EgAgB and myeloid cells, influencing the cytokine response induced during macrophage activation.

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