Research Article The Macrophage Galactose-Type Lectin-1 (MGL1) Recognizes Taenia crassiceps Antigens, Triggers Intracellular Signaling, and Is Critical for Resistance to This Infection

Copyright © 2015 Daniel Montero-Barrera et al.This is an open access article distributed under the Creative CommonsAttribution License, which permits unrestricted use, distribution, and reproduction in anymedium, provided the originalwork is properly cited. 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 structureswhich contain galactose residues, and it is selectively expressed on immatureDCs andmacrophages.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 ofWTmacrophages 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 respons