Effect of monovalent and divalent cations on Streptococcus thermophilus adhesion on human erythrocytes
Abstract
Bacterial adhesion to quite a few materials had been successfully described in terms of the interaction of the colloidal forces caused by the physical-chemical properties of bacteria and surfaces. An important factor, influencing the adhesion processes, is physical-chemical characteristics of the medium, in particular, the presence of monovalent and divalent cations therein. The dependence of adhesion of Streptococcus thermophilus microorganisms to human erythrocytes on the concentration of monovalent (Na+) and divalent (Са2+, Mg2+) cations has been studied. It is shown that the dependence behavior of adhesion of S.thermophilus microorganisms to human erythrocytes on the ionic strength of suspending solution is in accordance with the extended DLVO theory. So, the reported results indicate that the nonspecific first stage plays an important role in the course of adhesion process and affect the possibility of occurrence of the second stage. At the same time, the divalent cations Mg2+ and Ca2+ in the investigated physiological range likely affect the second, irreversible stage of the adhesive process, affecting the charge of adhesion molecules
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Gagneux P, Cheriyan M, Hurtado-Ziola N, et a. Human-specific regulation of α2–6-linked sialic acids. J Biol Chem. 2003; 278: 48245–50.
Evans DG, Evans DJ. Adhesion properties of Helicobacter pilori. Methods in Enzimology. 1995; 253: 336–60.
Marshall KC, Stout R, Mitchell R. Mechanism of the initial events in the sorption of marine bacteria to surfaces. J Gen Microbiol. 1971; 68: 337–48.
Carnazza S. New Advances in Cell Adhesion Technology Nanoparticles and Nanodevices in Biological Applications. Lecture Notes in Nanoscale Science and Technology. Berlin-Heidelberg: Springer-Verlag; 2009. 4: 69–130.
Israelachvili J. Intermolecular and Surface forces. Burlington: Academic Press; 2011. 674 p.
Bos R, van der Mei HC, Busscher HJ. Physico-chemistry of initial microbial adhesive interactions – its mechanisms and methods for study. FEMS Microbiol Rev. 1999; 23: 179–230.
Neu TR, Marshall KC. Bacterial polymers: Physico-chemical aspects of their interactions at interfaces. J Biomater Appl. – 1990; 5: 107–33.
van Oss C. J. Energetics of cell-cell and cell-biopolymer interactions. Cell Biophys. 1989; 14: 1–16.
An YH, Friedman RJ. Concise review of mechanisms of bacterial adhesion to biomaterial surfaces. J Biomed Mat. 1998; 43: 338–48.
Morra M, Cassinelli C. Bacterial adhesion to polymer surfaces: a critical review of surface thermodynamic approaches. J Biomater Sci Polymer Ed. 1997; 9: 55–74.
Cunliffe D, Smart CA, Alexander C, Vulfson EN. Bacterial adhesion at synthetic surfaces. Appl Environ Microbiol. 1999; 65: 4995–5002.
van Loosdrecht MCM, Lyklemam J, Norde W, Zehnder AJB. Hydrophobic and electrostatic parameters in bacterial adhesion Aquatic Sci. 1990; 52: 103–13.
Vadillo-Rodrıguez V, Busschera HJ, van der Mei HC, et al. Role of lactobacillus cell surface hydrophobicity as probed by AFM in adhesion to surfaces at low and high ionic strength. Colloids and Surfaces B: Biointerfaces. 2005; 41: 33–41.
Bos R, van der Mei HC, Busscher HJ. Influence of ionic strength and substratum hydrophobicity on the co-adhesion of oral microbial pairs. Miсrobiology. 1996; 142: 2355–61.
Vadillo-Rodrıguez V, Busscher HJ, Norde W, et al. Dynamic cell surface hydrophobicity of Lactobacillus strains with and without surface layer proteins. J Bacteriology. 2004; 186: 6647–50.
Martinez-Gil M, Romero D, Kolter R, Espinosa-Urgela M. Calcium causes multimerization of the large adhesin LapF and modulates biofilm formation by Pseudomonas putida. J Bacteriol. 2012; 194: 6782–9.
Arrizubieta MJ, Toledo-Arana A, Amorena B, et al. Calcium inhibits Bap-dependent multicellular behavior in Staphylococcus aureus. J Bacteriol. 2004; 186: 7490–8.
Yousef-Coronado F, Espinosa-Urgel M. In silico analysis of large microbial surface proteins. Res Microbiol. 2007; 158: 545–50.
Herrenknecht K. Cadherins / K. Herrenknecht // Molecular biology of cell adhesion molecules. Ed. M. A. Horton. New York: John Wiley; 1996. p. 45–69.
Driscoll PC, Cyster JG, Campbell ID, Williams AF. Structure of domain 1 of rat T lymphocyte CD2 antigen. Nature. 1991; 353: 762–5.
Blattman JN, Greenberg PD. Cancer immunotherapy: A treatment for the masses. Science. 2004; 305: 200–5.
van der Merwe PA, McNamee PN, Davies EA, et al. Topology of the CD2–CD48 cell-adhesion molecule complex: Implications for antigen recognition by T cells. Curr Biol. 1995; 5: 74–84.
Jones LM, Yang W, Maniccia AW, et al. Rational design of a novel calcium-binding site adjacent to the ligand-binding site on CD2 increases its CD48 affinity. Protein Science. 2008; 17: 439–49.
Chen HA, Pfuhl M, McAlister MS, Driscoll PC. Determination of pKa values of carboxyl groups in the N-terminal domain of rat CD2: Anomalous pKa of a glutamate on the ligand-binding surface. Biochemistry. 2000; 39: 6814–24.
Davis SJ, Davies EA, Tucknott MG, et al. The role of charged residues mediating low affinity protein–protein recognition at the cell surface by CD2. Proc Natl Acad Sci. 1998; 95: 5490–4.
Yang W, Lee HW, Hellinga H, Yang JJ. Structural analysis, identification, and design of calcium-binding sites in proteins. Proteins. 2002; 47: 344–56.
Marsden BJ, Shaw GS, Sykes BD. Calcium binding proteins. Elucidating the contributions to calcium affinity from an analysis of species variants and peptide fragments. Biochem Cell Biol. – 1990; 68: 587–601.
. Boyd CD, Chatterjee D, Sondermann H, O’Toole GA. LapG, required for modulating biofilm formation by Pseudomonas fluorescens Pf0-1, is a calciumdependent protease. J Bacteriol. – 2012; 194: 4406–14.
Cruz LF, Cobine PA, De La Fuente L. Calcium increases surface attachment, biofilm formation, and twitching motility in Xylella fastidiosa. Appl Environ Microbiol. 2012; 78: 1321–31.
Garrison-Schilling KL, et al. Calcium promotes exopolysaccharide phase variation and biofilm formation of the resulting phase variants in the human pathogen Vibrio vulnificus. Environ Microbiol. 2011; 13: 643–54.
Theunissen S, et al. The 285 kDa Bap/RTX hybrid cell surface protein (SO4317) of Shewanella oneidensis MR- 1 is a key mediator of biofilm formation. Res Microbiol. 2010; 161: 144–52.
Mahalingam B, Ajroud K, Alonso JLS, et al. Stable Coordination of the Inhibitory Ca2+ Ion at the Metal Ion-Dependent Adhesion Site in Integrin CD11b/CD18 by an Antibody-Derived Ligand Aspartate: Implications for Integrin Regulation and Structure-Based Drug Design. J Immun. 2011; 187: 6393–401.
Dudev T, Lim C. Monodentate versus bidentate carboxylate binding in magnesium and calcium proteins: what are the basic principles? J Phys Chem. 2004; 108: 4546–57.
Marcus Y. Ionic radii in aqueous solutions. Chem Rev. 1988; 88: 1475–98.
San Sebastian E, Mercero JM, Stote RH. et al. On the affinity regulation of the metal-ion-dependent adhesion sites in integrins. J Am Chem Soc. 2006; 128: 3554–63.
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