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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-4R α , 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.

biomed research international

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

The Macrophage Galactose-Type Lectin-1 (MGL1) RecognizesTaenia crassicepsAntigens, Triggers Intracellular Signaling, and Is Critical for Resistance to This Infection