Galectin-3 binds lactosaminylated lipooligosaccharides from Neisseria gonorrhoeae and is selectively expressed by mucosal epithelial cells that are infected |
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Authors: | John Constance M Jarvis Gary A Swanson Karen V Leffler Hakon Cooper Morris D Huflejt Margaret E Griffiss J McLeod |
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Affiliation: | Center for Immunochemistry and VA Medical Center, San Francisco, CA 94121, USA.;Department of Laboratory Medicine, University of California San Francisco, CA 94143, USA.;Department of Medical Microbiology, Section for Clinical Immunology, Lund University, S-22362, Lund, Sweden.;Department of Medical Microbiology and Immunology, Southern Illinois University, Springfield, Illinois 62708, USA.;Burnham Institute, La Jolla, CA 92037, USA. |
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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 (Lc2 or Lac), paraglobosyl (nLc4; LNnT; lacto-N-neotetraose), gangliosyl (IV3GalNAcnLc4), and neolactohexaosyl (nLc6, lactonorhexaosyl) oligosaccharides. All but gangliosyl LOS terminate in beta-galactoside. Galectin-3 had the highest affinity for the nLc6 LOS, which is made by a strain that is highly infectious for the male urethra, but also bound nLc4 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. |
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