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Galectin-3, a marker for vacuole lysis by invasive pathogens

Paz, Irit; Sachse, Martin; Dupont, Nicolas; Mounier, Joelle; Cederfur, Cecilia LU ; Enninga, Jost; Leffler, Hakon LU ; Poirier, Francoise; Prevost, Marie-Christine and Lafont, Frank, et al. (2010) In Cellular Microbiology 12(4). p.530-544
Abstract
P>Shigella bacteria invade macrophages and epithelial cells and following internalization lyse the phagosome and escape to the cytoplasm. Galectin-3, an abundant protein in macrophages and epithelial cells, belongs to a family of beta-galactoside-binding proteins, the galectins, with many proposed functions in immune response, development, differentiation, cancer and infection. Galectins are synthesized as cytosolic proteins and following non-classical secretion bind extracellular beta-galactosides. Here we analysed the localization of galectin-3 following entry of Shigella into the cytosol and detected a striking phenomenon. Very shortly after bacterial invasion, intracellular galectin-3 accumulated in structures in vicinity to... (More)
P>Shigella bacteria invade macrophages and epithelial cells and following internalization lyse the phagosome and escape to the cytoplasm. Galectin-3, an abundant protein in macrophages and epithelial cells, belongs to a family of beta-galactoside-binding proteins, the galectins, with many proposed functions in immune response, development, differentiation, cancer and infection. Galectins are synthesized as cytosolic proteins and following non-classical secretion bind extracellular beta-galactosides. Here we analysed the localization of galectin-3 following entry of Shigella into the cytosol and detected a striking phenomenon. Very shortly after bacterial invasion, intracellular galectin-3 accumulated in structures in vicinity to internalized bacteria. By using immuno-electron microscopy analysis we identified galectin-3 in membranes localized in the phagosome and in tubules and vesicles that derive from the endocytic pathway. We also demonstrated that the binding of galectin-3 to host N-acetyllactosamine-containing glycans, was required for forming the structures. Accumulation of the structures was a type three secretion system-dependent process. More specifically, existence of structures was strictly dependent upon lysis of the phagocytic vacuole and could be shown also by Gram-positive Listeria and Salmonella sifA mutant. We suggest that galectin-3-containing structures may serve as a potential novel tool to spot vacuole lysis. (Less)
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Contribution to journal
publication status
published
subject
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Cellular Microbiology
volume
12
issue
4
pages
530 - 544
publisher
Wiley-Blackwell
external identifiers
  • wos:000275330600009
  • scopus:77954271859
ISSN
1462-5814
DOI
10.1111/j.1462-5822.2009.01415.x
language
English
LU publication?
yes
id
023476a6-9649-4db6-a033-b8df0fe1a9bd (old id 1589127)
date added to LUP
2010-04-20 13:57:01
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2018-07-01 03:21:00
@article{023476a6-9649-4db6-a033-b8df0fe1a9bd,
  abstract     = {P>Shigella bacteria invade macrophages and epithelial cells and following internalization lyse the phagosome and escape to the cytoplasm. Galectin-3, an abundant protein in macrophages and epithelial cells, belongs to a family of beta-galactoside-binding proteins, the galectins, with many proposed functions in immune response, development, differentiation, cancer and infection. Galectins are synthesized as cytosolic proteins and following non-classical secretion bind extracellular beta-galactosides. Here we analysed the localization of galectin-3 following entry of Shigella into the cytosol and detected a striking phenomenon. Very shortly after bacterial invasion, intracellular galectin-3 accumulated in structures in vicinity to internalized bacteria. By using immuno-electron microscopy analysis we identified galectin-3 in membranes localized in the phagosome and in tubules and vesicles that derive from the endocytic pathway. We also demonstrated that the binding of galectin-3 to host N-acetyllactosamine-containing glycans, was required for forming the structures. Accumulation of the structures was a type three secretion system-dependent process. More specifically, existence of structures was strictly dependent upon lysis of the phagocytic vacuole and could be shown also by Gram-positive Listeria and Salmonella sifA mutant. We suggest that galectin-3-containing structures may serve as a potential novel tool to spot vacuole lysis.},
  author       = {Paz, Irit and Sachse, Martin and Dupont, Nicolas and Mounier, Joelle and Cederfur, Cecilia and Enninga, Jost and Leffler, Hakon and Poirier, Francoise and Prevost, Marie-Christine and Lafont, Frank and Sansonetti, Philippe},
  issn         = {1462-5814},
  language     = {eng},
  number       = {4},
  pages        = {530--544},
  publisher    = {Wiley-Blackwell},
  series       = {Cellular Microbiology},
  title        = {Galectin-3, a marker for vacuole lysis by invasive pathogens},
  url          = {http://dx.doi.org/10.1111/j.1462-5822.2009.01415.x},
  volume       = {12},
  year         = {2010},
}