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Galectin-3 binds lactosaminylated lipooligosaccharides from Neisseria gonorrhoeae and is selectively expressed by mucosal epithelial cells that are infected

John, Constance M; Jarvis, Garry A; Swanson, Karen V; Leffler, Hakon LU ; Cooper, Morris D; Huflejt, Margret E and Mc Leod Griffiss, J (2002) In Cellular Microbiology 4(10). p.649-661
Abstract
Galectins are a family of beta-galactoside binding proteins that have been proposed as host receptors for bacteria because beta-galactoside carbohydrates are common in bacterial membrane glycolipid lipooligosaccharides (LOS) and lipopolysaccharides. We investigated the interaction of galectin-3 with gonococcal LOS that make lactosyl (Lc(2) or Lac), paraglobosyl (nLc(4) ; LNnT; lacto-N -neotetraose), gangliosyl (IV3 GalNAcnLc(4) ), and neolactohexaosyl (nLc(6) , lactonorhexaosyl) oligosaccharides. All but gangliosyl LOS terminate in beta-galactoside. Galectin-3 had the highest affinity for the nLc(6) LOS, which is made by a strain that is highly infectious for the male urethra, but also bound nLc(4) LOS and to a Lac LOS. The lacto-N... (More)
Galectins are a family of beta-galactoside binding proteins that have been proposed as host receptors for bacteria because beta-galactoside carbohydrates are common in bacterial membrane glycolipid lipooligosaccharides (LOS) and lipopolysaccharides. We investigated the interaction of galectin-3 with gonococcal LOS that make lactosyl (Lc(2) or Lac), paraglobosyl (nLc(4) ; LNnT; lacto-N -neotetraose), gangliosyl (IV3 GalNAcnLc(4) ), and neolactohexaosyl (nLc(6) , lactonorhexaosyl) oligosaccharides. All but gangliosyl LOS terminate in beta-galactoside. Galectin-3 had the highest affinity for the nLc(6) LOS, which is made by a strain that is highly infectious for the male urethra, but also bound nLc(4) LOS and to a Lac LOS. The lacto-N -neotetraose tetrasaccharide was a more potent inhibitor of galectin-3 binding to LOS than either lactose or N -acetyllactosamine. The relative affinity of galectin-3 for gonococci mirrored its affinity for purified LOS. Western blot analysis revealed expression of galectin-3 by human endometrial adenocarcinoma and prostatic epithelial cells that can be invaded by gonococci. Immunohistochemistry of human fallopian tube epithelium showed localized expression of galectin-3 by non-ciliated cells, the specific cell gonococci invade in this tissue. We conclude that because of its location and affinity for gonococcal LOS galectin-3 could play a role in gonococcal infection. (Less)
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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Cellular Microbiology
volume
4
issue
10
pages
649 - 661
publisher
Wiley-Blackwell
external identifiers
  • wos:000178480600003
  • pmid:12366402
  • scopus:0036800448
ISSN
1462-5814
DOI
10.1046/j.1462-5822.2002.00219.x
language
English
LU publication?
yes
id
d4b52e81-51bd-4626-b01e-f88758b1c36a (old id 326214)
date added to LUP
2007-10-31 13:16:24
date last changed
2017-09-17 04:28:44
@article{d4b52e81-51bd-4626-b01e-f88758b1c36a,
  abstract     = {Galectins are a family of beta-galactoside binding proteins that have been proposed as host receptors for bacteria because beta-galactoside carbohydrates are common in bacterial membrane glycolipid lipooligosaccharides (LOS) and lipopolysaccharides. We investigated the interaction of galectin-3 with gonococcal LOS that make lactosyl (Lc(2) or Lac), paraglobosyl (nLc(4) ; LNnT; lacto-N -neotetraose), gangliosyl (IV3 GalNAcnLc(4) ), and neolactohexaosyl (nLc(6) , lactonorhexaosyl) oligosaccharides. All but gangliosyl LOS terminate in beta-galactoside. Galectin-3 had the highest affinity for the nLc(6) LOS, which is made by a strain that is highly infectious for the male urethra, but also bound nLc(4) LOS and to a Lac LOS. The lacto-N -neotetraose tetrasaccharide was a more potent inhibitor of galectin-3 binding to LOS than either lactose or N -acetyllactosamine. The relative affinity of galectin-3 for gonococci mirrored its affinity for purified LOS. Western blot analysis revealed expression of galectin-3 by human endometrial adenocarcinoma and prostatic epithelial cells that can be invaded by gonococci. Immunohistochemistry of human fallopian tube epithelium showed localized expression of galectin-3 by non-ciliated cells, the specific cell gonococci invade in this tissue. We conclude that because of its location and affinity for gonococcal LOS galectin-3 could play a role in gonococcal infection.},
  author       = {John, Constance M and Jarvis, Garry A and Swanson, Karen V and Leffler, Hakon and Cooper, Morris D and Huflejt, Margret E and Mc Leod Griffiss, J},
  issn         = {1462-5814},
  language     = {eng},
  number       = {10},
  pages        = {649--661},
  publisher    = {Wiley-Blackwell},
  series       = {Cellular Microbiology},
  title        = {Galectin-3 binds lactosaminylated lipooligosaccharides from Neisseria gonorrhoeae and is selectively expressed by mucosal epithelial cells that are infected},
  url          = {http://dx.doi.org/10.1046/j.1462-5822.2002.00219.x},
  volume       = {4},
  year         = {2002},
}