TY - JOUR
T1 - The macrophage galactose-type lectin-1 (MGL1) recognizes taenia crassiceps antigens, triggers intracellular signaling, and is critical for resistance to this infection
AU - Montero-Barrera, Daniel
AU - Valderrama-Carvajal, Héctor
AU - Terrazas, César A.
AU - Rojas-Hernández, Saúl
AU - Ledesma-Soto, Yadira
AU - Vera-Arias, Laura
AU - Carrasco-Yépez, Maricela
AU - Gómez-García, Lorena
AU - Martínez-Saucedo, Diana
AU - Becerra-Díaz, Mireya
AU - Terrazas, Luis I.
N1 - Publisher Copyright:
© 2015 Daniel Montero-Barrera et al.
PY - 2015/1/15
Y1 - 2015/1/15
N2 - C-type lectins are multifunctional sugar-binding molecules expressed on dendritic cells (DCs) and macrophages that internalize antigens for processing and presentation. Macrophage galactose-type lectin 1 (MGL1) recognizes glycoconjugates expressing Lewis X structures which contain galactose residues, and it is selectively expressed on immature DCs and macrophages. Helminth parasites contain large amounts of glycosylated components, which play a role in the immune regulation induced by such infections. Macrophages from MGL1-/- mice showed less binding ability toward parasite antigens than their wild-type (WT) counterparts. Exposure of WT macrophages to T. crassiceps antigens triggered tyrosine phosphorylation signaling activity, which was diminished in MGL1-/- macrophages. Following T. crassiceps infection, MGL1-/- mice failed to produce significant levels of inflammatory cytokines early in the infection compared to WT mice. In contrast, MGL1-/- mice developed a Th2-dominant immune response that was associated with significantly higher parasite loads, whereas WT mice were resistant. Flow cytometry and RT-PCR analyses showed overexpression of the mannose receptors, IL-4Rα, PDL2, arginase-1, Ym1, and RELM-α on MGL1-/- macrophages. These studies indicate that MGL1 is involved in T. crassiceps recognition and subsequent innate immune activation and resistance.
AB - C-type lectins are multifunctional sugar-binding molecules expressed on dendritic cells (DCs) and macrophages that internalize antigens for processing and presentation. Macrophage galactose-type lectin 1 (MGL1) recognizes glycoconjugates expressing Lewis X structures which contain galactose residues, and it is selectively expressed on immature DCs and macrophages. Helminth parasites contain large amounts of glycosylated components, which play a role in the immune regulation induced by such infections. Macrophages from MGL1-/- mice showed less binding ability toward parasite antigens than their wild-type (WT) counterparts. Exposure of WT macrophages to T. crassiceps antigens triggered tyrosine phosphorylation signaling activity, which was diminished in MGL1-/- macrophages. Following T. crassiceps infection, MGL1-/- mice failed to produce significant levels of inflammatory cytokines early in the infection compared to WT mice. In contrast, MGL1-/- mice developed a Th2-dominant immune response that was associated with significantly higher parasite loads, whereas WT mice were resistant. Flow cytometry and RT-PCR analyses showed overexpression of the mannose receptors, IL-4Rα, PDL2, arginase-1, Ym1, and RELM-α on MGL1-/- macrophages. These studies indicate that MGL1 is involved in T. crassiceps recognition and subsequent innate immune activation and resistance.
UR - http://www.scopus.com/inward/record.url?scp=84947650569&partnerID=8YFLogxK
U2 - 10.1155/2015/615865
DO - 10.1155/2015/615865
M3 - Artículo
SN - 2314-6133
VL - 2015
JO - BioMed Research International
JF - BioMed Research International
M1 - 615865
ER -