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Lactoferrin binding properties of Vibrio cholerae
F Ascencio1, A Ljungh, T Wadström
1Department of Medical Microbiology, University of Lund, Sweden.
Microbios
|January 1, 1992
Summary
Vibrio cholerae binds lactoferrin, with some strains showing significant binding. Proteolytic activity on the bacterial surface alters binding properties, favoring other iron-binding proteins.
Area of Science:
- Microbiology
- Bacterial Pathogenesis
- Protein-Ligand Interactions
Background:
- Lactoferrin is an iron-binding glycoprotein crucial in innate immunity.
- Vibrio cholerae is a non-invasive bacterial pathogen.
- Understanding bacterial interactions with host proteins is vital for pathogenesis research.
Purpose of the Study:
- To investigate the lactoferrin binding properties of Vibrio cholerae strains.
- To characterize the influence of bacterial surface proteases on lactoferrin binding.
Main Methods:
- Screening of fifty Vibrio cholerae strains for lactoferrin binding using 125I-labelled lactoferrin.
- Displacement assays with unlabelled lactoferrin and other iron-binding proteins.
- Assessing the effect of monosaccharides and other glycoproteins on binding.
- Investigating cell surface proteolytic activity of V. cholerae 623.
Main Results:
- 10% of V. cholerae strains bound 125I-lactoferrin; 40% of bound lactoferrin was displaceable by unlabelled lactoferrin.
- Ferritin, transferrin, hemoglobin, and myoglobin showed lesser inhibition of lactoferrin binding.
- Monosaccharides and other glycoproteins also inhibited binding to a lesser extent.
- V. cholerae 623 exhibited surface proteolytic activity, cleaving bound lactoferrin and promoting binding of other proteins.
Conclusions:
- Vibrio cholerae possesses mechanisms for interacting with lactoferrin, though binding varies among strains.
- Proteolytic activity on the V. cholerae surface can modify protein-binding profiles, potentially influencing host-pathogen interactions.