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Novel interactions of glycosaminoglycans and bacterial glycolipids mediate binding of enterococci to human cells.

ABSTRACT: Enterococcus faecalis is among the most important nosocomial pathogens. The intestinal mucosa is considered to be the main site used by these bacteria for entrance and dissemination. A better understanding of the mechanisms involved in colonization and invasion of enterococci may help to devise methods to prevent infections in hospitalized patients. Glycosaminoglycans, which are present on the surface of all eukaryotic cells, were investigated with regard to their role as host receptors for adhesion of E. faecalis. Competitive binding assays, enzymatic digestion, and reduction of the sulfation of the glycosaminoglycan chains indicated that heparin and heparan sulfate, but not chondroitin sulfate B, played important roles in adhesion of E. faecalis 12030 to Caco2 cells. By using proteinases and carbohydrate oxidation by sodium meta-periodate to modify the bacterial surface, it could be demonstrated that a sugar-containing molecule rather than a protein is the bacterial ligand mediating adhesion to eukaryotic cells. Preincubation of Caco2 cells with the enterococcal glycolipid diglucosyldiacylglycerol but not other carbohydrate cell wall components inhibited bacterial binding. These results may indicate that heparin and/or heparan sulfate on host epithelial cells and diglucosyldiacylglycerol, either itself or as a partial structure of lipoteichoic acid, are involved in enterococcal adhesion to colonic epithelia, the first step in translocation from the intestinal tract.

SUBMITTER: Sava IG

PROVIDER: S-EPMC2709396 | biostudies-literature | 2009 Jul

REPOSITORIES: biostudies-literature

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Novel interactions of glycosaminoglycans and bacterial glycolipids mediate binding of enterococci to human cells.

Sava Irina G IG Zhang Fuming F Toma Ioana I Theilacker Christian C Li Boyangzhi B Baumert Thomas F TF Holst Otto O Linhardt Robert J RJ Huebner Johannes J

The Journal of biological chemistry 20090423 27

Enterococcus faecalis is among the most important nosocomial pathogens. The intestinal mucosa is considered to be the main site used by these bacteria for entrance and dissemination. A better understanding of the mechanisms involved in colonization and invasion of enterococci may help to devise methods to prevent infections in hospitalized patients. Glycosaminoglycans, which are present on the surface of all eukaryotic cells, were investigated with regard to their role as host receptors for adhe ...[more]

PMID: 19395379

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Project description:Virus entry into host cells is a complex process that is largely regulated by access to specific cellular receptors. Human adenoviruses (HAdVs) and many other viruses use cell adhesion molecules such as the coxsackievirus and adenovirus receptor (CAR) for attachment to and entry into target cells. These molecules are rarely expressed on the apical side of polarized epithelial cells, which raises the question of how adenoviruses-and other viruses that engage cell adhesion molecules-enter polarized cells from the apical side to initiate infection. We have previously shown that species C HAdVs utilize lactoferrin-a common innate immune component secreted to respiratory mucosa-for infection via unknown mechanisms. Using a series of biochemical, cellular, and molecular biology approaches, we mapped this effect to the proteolytically cleavable, positively charged, N-terminal 49 residues of human lactoferrin (hLF) known as human lactoferricin (hLfcin). Lactoferricin (Lfcin) binds to the hexon protein on the viral capsid and anchors the virus to an unknown receptor structure of target cells, resulting in infection. These findings suggest that HAdVs use distinct cell entry mechanisms at different stages of infection. To initiate infection, entry is likely to occur at the apical side of polarized epithelial cells, largely by means of hLF and hLfcin bridging HAdV capsids via hexons to as-yet-unknown receptors; when infection is established, progeny virions released from the basolateral side enter neighboring cells by means of hLF/hLfcin and CAR in parallel.IMPORTANCE Many viruses enter target cells using cell adhesion molecules as receptors. Paradoxically, these molecules are abundant on the lateral and basolateral side of intact, polarized, epithelial target cells, but absent on the apical side that must be penetrated by incoming viruses to initiate infection. Our study provides a model whereby viruses use different mechanisms to infect polarized epithelial cells depending on which side of the cell-apical or lateral/basolateral-is attacked. This study may also be useful to understand the biology of other viruses that use cell adhesion molecules as receptors.

Dataset Information

Novel interactions of glycosaminoglycans and bacterial glycolipids mediate binding of enterococci to human cells.

Publications

Novel interactions of glycosaminoglycans and bacterial glycolipids mediate binding of enterococci to human cells.

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