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Published on: December 17, 2011
Adhesion of Yersinia enterocolitica to purified rabbit and human intestinal mucin
Abstract:
Interactions between Yersinia enterocolitica and purified intestinal mucins from rabbit and humans were investigated. Plasmid-bearing virulent organisms (but not plasmid-free nonvirulent bacteria) bound well to both mucins, suggesting that adherence was controlled by the virulence plasmid. Examination of binding to 14 different preparations of purified human intestinal mucin (8 preparations obtained from normal subjects and 6 samples from patients with cystic fibrosis) revealed no differences between normal and cystic fibrotic mucins in ability to serve as a binding substrate for virulent Y. enterocolitica. Analyses of binding curves suggested the presence of a single type of noninteracting receptor for Y. enterocolitica in both rabbit and human mucins with similar (but not necessarily identical) structures. Virulent bacteria bound to polystyrene through hydrophobic interactions that could be disrupted by treating the organisms with tetramethyl urea. In contrast, binding of plasmid-bearing Y. enterocolitica to intestinal mucin was not susceptible to tetramethyl urea and therefore does not appear to involve hydrophobic interactions. Prior incubation of organisms with mucin significantly inhibited binding to polystyrene, suggesting that mucin can mask hydrophobic adhesins on the bacterial surface. Hapten inhibition studies revealed that the monosaccharides galactose and N-acetylgalactosamine and the disaccharide lactose could markedly reduce (but not abolish) bacterial adherence to mucin but other monosaccharides and the RGD peptide had no effect on mucin binding. We conclude that virulent Y. enterocolitica is capable of interacting with the carbohydrate moiety of intestinal mucin. These interactions appear to be plasmid mediated and not hydrophobic.
Insights
Virulent Yersinia enterocolitica binds to intestinal mucins via plasmid-mediated interactions with carbohydrate structures, not hydrophobic forces. This binding is unaffected by cystic fibrosis, suggesting a common interaction mechanism.
Area of Science:
- Microbiology
- Glycobiology
- Infectious Diseases
Background:
- Yersinia enterocolitica is a pathogen that interacts with the host intestinal environment.
- Intestinal mucins form a protective layer, and their interaction with bacteria is crucial for colonization and pathogenesis.
- The role of the Yersinia virulence plasmid in bacterial adherence to host tissues requires further elucidation.
Purpose of the Study:
- To investigate the interaction between virulent Yersinia enterocolitica and purified intestinal mucins.
- To determine the nature of the binding, including the role of the virulence plasmid and specific molecular interactions.
- To compare mucin binding properties between normal and cystic fibrosis subjects.
Main Methods:
- Investigated binding of plasmid-bearing and plasmid-free Yersinia enterocolitica to purified rabbit and human intestinal mucins.
- Utilized tetramethyl urea to assess the role of hydrophobic interactions in bacterial binding.
- Performed hapten inhibition studies using monosaccharides and peptides to identify specific binding moieties.
Main Results:
- Plasmid-bearing virulent Yersinia enterocolitica exhibited significant binding to both rabbit and human mucins, unlike plasmid-free strains.
- Bacterial binding to mucin was not hydrophobic and was unaffected by tetramethyl urea treatment.
- Binding to mucin was inhibited by galactose, N-acetylgalactosamine, and lactose, indicating interaction with the carbohydrate moiety.
- No difference in binding was observed between normal and cystic fibrosis mucins.
Conclusions:
- Virulent Yersinia enterocolitica interacts with the carbohydrate component of intestinal mucins in a plasmid-dependent manner.
- The interaction is not mediated by hydrophobic forces, and mucin may mask bacterial hydrophobic adhesins.
- Cystic fibrosis mucins do not exhibit altered binding characteristics for virulent Yersinia enterocolitica compared to normal mucins.
