Open AccessAmaranthus leucocarpus lectin recognizes a moesin‐like O‐glycoprotein and costimulates murine CD3‐activated CD4 + T cells
Author(s) -
ArenasDel Ángel Maria,
LegorretaHerrera Martha,
MendozaHernández Guillermo,
Garfias Yonathan,
Chávez Raul,
Zenteno Edgar,
Lascurain Ricardo
Publication year - 2015
Publication title -
immunity, inflammation and disease
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.918
H-Index - 18
ISSN - 2050-4527
DOI - 10.1002/iid3.58
Subject(s) - moesin , microbiology and biotechnology , cd28 , biology , cd3 , lipid raft , t cell , glycoprotein , antigen , chemistry , cd8 , biochemistry , cell , immune system , signal transduction , ezrin , cytoskeleton , immunology
The Galβ1,3GalNAcα1,O‐Ser/Thr specific lectin from Amaranthus leucocarpus ( ALL ) binds a ∼70 kDa glycoprotein on murine T cell surface. We show that in the absence of antigen presenting cells, murine CD4 + T cells activated by an anti‐CD3 antibody plus ALL enhanced cell proliferation similar to those cells activated via CD3/CD28 at 48 h of culture. Moreover, ALL induced the production of IL‐4, IL‐10, TNF‐alpha, and TGF‐beta in CD3‐activated cells. Proteomic assay using two‐dimensional electrophoresis and far‐Western blotting, ALL recognized two prominent proteins associated to the lipid raft microdomains in CD3/CD28‐activated CD4 + T cells. By mass spectrometry, the peptide fragments from ALL ‐recognized proteins showed sequences with 33% homology to matricin (gi|347839 NCBInr) and 41% identity to an unnamed protein related to moesin (gi|74186081 NCBInr). Confocal microscopy analysis of CD3/CD28‐activated CD4 + T cells confirmed that staining by ALL colocalized with anti‐moesin FERM domain antibody along the plasma membrane and in the intercellular contact sites. Our findings suggest that a moesin‐like O‐glycoprotein is the ALL ‐recognized molecule in lipid rats, which induces costimulatory signals on CD4 + T cells.