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Intestinal mucins: the binding sites for Salmonella typhimurium
D B Vimal1, M Khullar, S Gupta
1Department of Experimental Medicine and Biotechnology, Postgraduate Institute of Medical Education and Research, Chandigarh, India.
Molecular and Cellular Biochemistry
|March 16, 2000
Summary
Salmonella typhimurium specifically binds to a 250 kDa intestinal mucus protein (Mucus-Rs), involving mannose interactions. This interaction is crucial for understanding enteric infections and bacterial adhesion mechanisms.
Area of Science:
- Gastroenterology
- Microbiology
- Biochemistry
Background:
- Mucus-bacterial interactions in the gut are not well understood.
- These interactions influence enteric infections.
Purpose of the Study:
- To investigate Salmonella typhimurium binding to rat intestinal mucus.
- To characterize the specific mucus protein involved in this binding.
Main Methods:
- Fractionation of mucus using sepharose CL-6B.
- Protein purification and characterization using SDS-PAGE.
- Analysis of sugar composition (GLC) and competitive binding assays.
Main Results:
- Salmonella typhimurium binds to a high molecular weight glycoprotein (Mucus-Rs).
- Virulent S. typhimurium shows significantly higher binding than avirulent strains.
- Binding involves mannose residues on the Mucus-Rs and bacterial pili.
Conclusions:
- S. typhimurium specifically binds to a 250 kDa neutral mucin (Mucus-Rs) in the intestinal tract.
- This interaction is mediated by adhesin-receptor mechanisms involving mannose.
- Understanding this binding is key to developing strategies against enteric infections.