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Galectin 8 targets damaged vesicles for autophagy to defend cells against bacterial invasion.

Autophagy defends the mammalian cytosol against bacterial infection. Efficient pathogen engulfment is mediated by cargo-selecting autophagy adaptors that rely on unidentified pattern-recognition or danger receptors to label invading pathogens as autophagy cargo, typically by polyubiquitin coating. Here we show in human cells that galectin 8 (also known as LGALS8), a cytosolic lectin, is a danger receptor that restricts Salmonella proliferation. Galectin 8 monitors endosomal and lysosomal integrity and detects bacterial invasion by binding host glycans exposed on damaged Salmonella-containing vacuoles. By recruiting NDP52 (also known as CALCOCO2), galectin 8 activates antibacterial autophagy. Galectin-8-dependent recruitment of NDP52 to Salmonella-containing vesicles is transient and followed by ubiquitin-dependent NDP52 recruitment. Because galectin 8 also detects sterile damage to endosomes or lysosomes, as well as invasion by Listeria or Shigella, we suggest that galectin 8 serves as a versatile receptor for vesicle-damaging pathogens. Our results illustrate how cells deploy the danger receptor galectin 8 to combat infection by monitoring endosomal and lysosomal integrity on the basis of the specific lack of complex carbohydrates in the cytosol.

Pubmed ID: 22246324


  • Thurston TL
  • Wandel MP
  • von Muhlinen N
  • Foeglein A
  • Randow F



Publication Data

February 16, 2012

Associated Grants

  • Agency: Medical Research Council, Id: MC_U105170648
  • Agency: Medical Research Council, Id: U.1051.03.011(78825)

Mesh Terms

  • Autophagy
  • Cell Proliferation
  • Cytoplasm
  • Cytoplasmic Vesicles
  • Endosomes
  • Galectins
  • HeLa Cells
  • Humans
  • Lysosomes
  • Nuclear Proteins
  • Salmonella Infections
  • Salmonella typhimurium