Galectin-3, a marker for vacuole lysis by invasive pathogens
(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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https://lup.lub.lu.se/record/1589127
- author
- organization
- publishing date
- 2010
- type
- Contribution to journal
- publication status
- published
- subject
- in
- Cellular Microbiology
- volume
- 12
- issue
- 4
- pages
- 530 - 544
- publisher
- John Wiley & Sons Inc.
- external identifiers
-
- wos:000275330600009
- scopus:77954271859
- pmid:19951367
- 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
- 2016-04-01 10:58:11
- date last changed
- 2025-10-14 11:22:29
@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 = {{John Wiley & Sons Inc.}},
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}},
doi = {{10.1111/j.1462-5822.2009.01415.x}},
volume = {{12}},
year = {{2010}},
}