Carbohydrate Recognition Mechanisms which Mediate Microbial Adherence to Mammalian Mucosal Surfaces(MEMBRANE PROTEINS IN CELLULAR INTERACTIONS)

  • MIRELMAN David
    Department of Biophysics and Unit for Molecular Biology of Parasitic Diseases, Weizmann Institute of Science
  • IZHAR Mordechai
    Department of Biophysics and Unit for Molecular Biology of Parasitic Diseases, Weizmann Institute of Science
  • ESHDAT Yuval
    Department of Biophysics and Unit for Molecular Biology of Parasitic Diseases, Weizmann Institute of Science

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Bacterial adherence to animal cell surfaces is interesting not only because of its relation to pathogenicity, but also because its studies provide insight into determinants of intercellular recognition. In order to colonize human mucosal surfaces, bacteria have to bind first to the epithelial cell surface, otherwise they will be discarded by host defense mechanisms. In many gram negative organisms, surface pili (adhesins) mediate their binding to epithelial cells. The adherence of numerous types of these organisms to a variety of eukaryotic cells (epithelial, phagocytes, yeasts or red blood cells) is mediated by type I pili that exhibit manonose binding activity. Pili polypeptide subunits obtained after dissociation with saturated guanidine HCl partially retained their mannose binding capacity. Mannose binding adhesins have also been found to be associated with the flagella of certain Escherichia coli and Serratia marcescens strains or with outer membranes of E. coli. The nature of the mannose containing glycoprotein receptors on the animal cells is still unknown. There is good reason to believe that mannose-specific attachment plays a role in infectivity as the administration of mannose derivatives was effective in diminishing experimental E. coli urinary tract infection in mice and certain types of diarrhea. Other types of bacterial pili known to mediate mannose-insensitive adherence to eukaryotic cells have been reported. Thus E. coli originating from human urinary tract infection have an affinity for glycolipids of the globoside series, and enterotoxicogenic strains having a different array of organelles which facilitate colonization, display affinity for certain ganglioside, as well as to yet unidentified receptors. Studies on the adherence of non pilated clinical isolates of Shigella flexneri to the colonic epithelial cells of guinea pigs revealed that their attachment could be specfically inhibited by fucose or glucose. However, in contrast to other known bacterial adherence mechanisms, the adhesin, that mediates the attachment of the bacteria to the mucosal surface, was detected not on the Shigella surface but as an intestial proteinous component that is released together with the mucus gel by the colonic epithelial cells. The intestinal adhesin binds to certain sugars of the bacterial lipopolysaccharide which serve as receptors, and it causes the agglutination of Shigella and other types of bacteria.

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