| Autor: |
John, Constance M., Jarvis, Gary A., Swanson, Karen V., Leffler, Hakon, Cooper, Morris D., Huflejt, Margaret E., Griffiss, J. McLeod |
| Předmět: |
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| Zdroj: |
Cellular Microbiology; Oct2002, Vol. 4 Issue 10, p649-662, 14p |
| Abstrakt: |
Summary Galectins are a family of β-galactoside binding proteins that have been proposed as host receptors for bacteria because β-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 (IV3 GalNAcnLc4 ), and neolactohexaosyl (nLc6 , lactonorhexaosyl) oligosaccharides. All but gangliosyl LOS terminate in β-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. [ABSTRACT FROM AUTHOR] |
| Databáze: |
Complementary Index |
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