Cytosolic galectin-3 and -8 regulate antibacterial autophagy through differential recognition of host glycans on damaged phagosomes

作者: I-Chun Weng , Hung-Lin Chen , Tzu-Han Lo , Wei-Han Lin , Huan-Yuan Chen

DOI: 10.1093/GLYCOB/CWY017

关键词:

摘要: While glycans are generally displayed on the cell surface or confined within lumen of organelles, they can become exposed to cytosolic milieu upon disruption organelle membrane by various stresses pathogens. Galectins a family β-galactoside-binding animal lectins synthesized and predominantly localized in cytosol. Recent research indicates that some galectins may act as "danger signal sensors" detecting unusual exposure Galectin-8 was shown promote antibacterial autophagy recognizing host ruptured vacuolar membranes interacting with adaptor protein NDP52. Galectin-3 also accumulates at damaged phagosomes containing bacteria; however, its functional consequence remains obscure. By studying mouse macrophages infected Listeria monocytogenes (LM), we showed endogenous galectin-3 protects intracellular LM suppressing autophagic response through N-glycan-dependent mechanism. Knock out gene resulted enhanced LC3 recruitment decreased bacterial replication, phenotype recapitulated when Galectin-8-deficient were depleted N-glycans. Moreover, explored concept alterations glycosylation extracellular factors be deciphered during process phagocytosis/endocytosis, followed rupture phagosomal/endosomal membrane. Notably, treatment cells sialidase, which removes sialic acid from glycans, increased accumulation galectin-8 phagosomes, led stronger anti-autophagic response. Our findings demonstrate sense changes modulate cellular differential recognition phagosomal membranes.

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