Cells of E. coli isolates from the gut of healthy volunteers (N=5) and patients with Crohn’s disease (N=5) and laboratory E. coli strain DH5α bound mucin in vitro in similar amounts ranging from 0.02 to 0.12 mg/mg of bacterial dry weight. Binding was evaluated by the decrease in optical absorption of mucin solution at 214 nm after incubation with bacteria. Detailed analysis of mucin binding by one of isolates showed that during incubation of 0.09 mg/ml bacteria in 0.15 M NaCl containing 0.1 mg/ml mucin at 25oC, maximum binding was reached in 30 min, while in the presence of 14 mM α-methyl mannoside, mucin binding decreased by 46% (p<0.05). Confocal microscopy revealed intensive binding of FITC-labeled mucin to the surface of a small number of bacterial cells. Mucin binding did not significantly affect zeta potential of bacteria and their energetic status assessed by ATP content; at the same time, ATP content in the extracellular environment slightly increased.
References
Agus A, Massier S, Darfeuille-Michaud A, Billard E, Barnich N. Understanding host-adherent-invasive Escherichia coli interaction in Crohn’s disease: opening up new therapeutic strategies. Biomed. Res. Int. 2014;2014. ID 567929. doi: https://doi.org/10.1155/2014/567929.
Ascencio F, Martinez-Arias W, Romero MJ, Wadström T. Analysis of the interaction of Aeromonas caviae, A. hydrophila and A. sobria with mucins. FEMS Immunol. Med. Microbiol. 1998;20(3):219-229.
Balabushevich NG, Lopez de Guerenu AV, Feoktistova NA, Volodkin D. Protein loading into porous CaCO3 microspheres: adsorption equilibrium and bioactivity retention. Phys. Chem. Chem. Phys. 2015;17(4):2523-2530.
Balabushevich NG, Pechenkin MA, Shibanova ED, Volodkin DV, Mikhalchik EV. Multifunctional polyelectrolyte microparticles for oral insulin delivery. Macromol. Biosci. 2013;13(10):1379-1388.
Bansil R, Turner BS. Mucin structure, aggregation, physiological functions and biomedical applications. Curr. Opin. Colloid Interface Sci. 2006;11:164-170.
Huang JY, Lee SM, Mazmanian SK. The human commensal Bacteroides fragilis binds intestinal mucin. Anaerobe. 2011;17(4):137-141.
Hytönen J, Haataja S, Isomäki P, Finne J. Identification of a novel glycoprotein-binding activity in Streptococcus pyogenes regulated by the mga gene. Microbiology. 2000;146(Pt 1): 31-39.
Kłodzińska E, Szumski M, Dziubakiewicz E, Hrynkiewicz K, Skwarek E, Janusz W, Buszewski B. Effect of zeta potential value on bacterial behavior during electrophoretic separation. Electrophoresis 2010;31(9):1590-1596.
Linden SK, Sutton P, Karlsson NG, Korolik V, McGuckin MA. Mucins in the mucosal barrier to infection. Mucosal Immunol. 2008;1(3):183-197.
Lomakina GY, Modestova YA, Ugarova NN. Bioluminescence assay for cell viability. Biochemistry (Mosc.) 2015;80(6):701-713.
McAuley JL, Linden SK, Png CW, King RM, Pennington HL, Gendler SJ, Florin TH, Hill GR, Korolik V, McGuckin MA. MUC1 cell surface mucin is a critical element of the mucosal barrier to infection. J. Clin. Invest. 2007;117(8):2313-2324.
Mossman KL, Mian MF, Lauzon NM, Gyles CL, Lichty B, Mackenzie R, Gill N, Ashkar AA. Cutting edge: FimH adhesin of type 1 fimbriae is a novel TLR4 ligand. J. Immunol. 2008;181(10):6702-6706.
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Translated from Byulleten’ Eksperimental’noi Biologii i Meditsiny, Vol. 165, No. 2, pp. 198-201, February, 2018
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Vakhrusheva, T.V., Baikova, Y.P., Balabushevich, N.G. et al. Binding of Mucin by E. coli from Human Gut. Bull Exp Biol Med 165, 235–238 (2018). https://doi.org/10.1007/s10517-018-4137-3
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DOI: https://doi.org/10.1007/s10517-018-4137-3