Galectin-3 Inhibits Galectin-8/Parkin-Mediated Ubiquitination of Group A Streptococcus.

摘要: Group A streptococcus (GAS) is an important human pathogen that causes a wide variety of cutaneous and systemic infections. Although originally thought to be extracellular bacterium, numerous studies have demonstrated GAS can trigger internalization into nonimmune cells escape from immune surveillance or antibiotic-mediated killing. Epithelial possess defense mechanism involving autophagy-mediated targeting killing within lysosome-fused autophagosomes. In endothelial cells, in contrast, we previously showed autophagy not sufficient for the present study, higher galectin-3 (Gal-3) expression lower Gal-8 than epithelial cells. The recruitment Gal-3 We further promotes replication diminishes ubiquitin, latter which critical protein sequestration. After knockdown colocalization Gal-8, parkin, ubiquitin-decorated significantly increased, as interaction E3 ligase. Furthermore, inhibition attenuates parkin; both parkin contribute ubiquitin elimination. Animal confirmed Gal-3-knockout mice develop less-severe skin damage detected only air pouch organs These results demonstrate inhibits by blocking recruitment, resulting cells.IMPORTANCE efficiently killed autophaosome compartment. However, that, spite LC-3 autophagic machinery this report, provide first evidence Gal-3, highly expressed blocks tagging inhibiting leading enhancement replication. also demonstration interact with ligase, resistance intracellular bacteria facilitating decoration chains. Our findings reveal differential levels between may different outcomes elimination survival growth these two types