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Adherence ofStaphylococcus epidermidis to human pharyngeal epithelial cells: Evidence for lipase-sensitive adhesin and glycoprotein receptor

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Abstract

The adherence of eight strains ofStaphylococcus epidermidis to human pharyngeal epithelial cells (PEC) was investigated. All bacterial strains were nonencapsulated and non-slime producers. Binding was mannose resistant and was not related to surface hydrophobicity and surface charge of bacteria. Adherence to epithelial cells was reduced four- to tenfold (P<0.01) on pretreatment of bacteria with lipase while neuraminidase, phospholipase C, trypsin, and sodium periodate did not alter their binding. The surface carbohydrate profile of bacteria was studied by monitoring adherence to Lectin-Sepharoses. The bacteria did not conform to any pattern, and there was no relation to strain variation. The pretreatment of PEC with trypsin and sodium metaperiodate produced a marked reduction in bacterial binding (three- to 25-fold, P<0.01), but neuraminidase, phospholipase C, and lipase did not have any such effect. These findings provide evidence that the receptors on the surface of PEC are glycoprotein in nature, while the bacterial adhesin is a lipase-sensitive material.

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Chugh, T.D., Burns, G.J., Shuhaiber, H.J. et al. Adherence ofStaphylococcus epidermidis to human pharyngeal epithelial cells: Evidence for lipase-sensitive adhesin and glycoprotein receptor. Current Microbiology 18, 109–112 (1989). https://doi.org/10.1007/BF01570834

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