Premium
Giardia lamblia binding immunoglobulin protein triggers maturation of dendritic cells via activation of TLR 4‐MyD88‐p38 and ERK 1/2 MAPK s
Author(s) -
Lee H.Y.,
Kim J.,
Noh H. J.,
Kim H.P.,
Park S.J.
Publication year - 2014
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.12119
Subject(s) - cd86 , biology , giardia lamblia , cd80 , tlr4 , western blot , antibody , microbiology and biotechnology , p38 mitogen activated protein kinases , immune system , mapk/erk pathway , t cell , signal transduction , cd40 , immunology , biochemistry , in vitro , gene , cytotoxic t cell
Summary Much remains unknown about the mammalian immune response to Giardia lamblia , a protozoan pathogen that causes diarrhoeal outbreaks. We fractionated protein extracts of G. lamblia trophozoites by Viva‐spin centrifugation, DEAE ion exchange and gel filtration chromatography. Resultant fractions were screened for antigenic molecules by western blots analysis using anti‐ G. lamblia antibodies (Abs), resulting in identification of G. lamblia binding immunoglobulin protein (GlBiP). Maturation of mouse dendritic cells (DCs) in response to recombinant GlBiP ( rGlBiP ) was detected by increased expression of surface molecules such as CD80, CD86 and MHC class II; these mature DCs, produced pro‐inflammatory cytokines (TNF‐α, IL‐12 and IL‐6). Especially, the truncated rGlBiP containing the heat‐shock protein 70 domain‐induced cytokine production from mouse DCs. rGlBiP ‐induced DC activation was initiated by TLR4 in a MyD88‐dependent way and occurred through activation of p38 and ERK1/2 MAPKs as well as increased activity of NF‐ κB and AP‐1. Moreover, CD4 + T cells stimulated with rGlBiP ‐treated DCs produced high levels of IL‐2 and IFN‐γ. Together, our results suggest that GlBiP contributes to maturation of DCs via activation of TLR4‐MyD88‐p38, ERK1/2 MAPK, NF‐κB and AP‐1.