Mediation of adherence of streptococci to human endothelial cells by complement S protein (vitronectin).
The role of S protein in the adherence of group A and G streptococci to human umbilical vein endothelial cells cultivated in 96-well microdilution plates was studied by utilizing fluorescein-labeled streptococci. The assay proved suitable for quantitative determination of bacterial adherence to cultured endothelial cells for all tested strains of streptococci. Only bacterial strains with significant S protein binding but weak fibronectin binding were included in these studies. Fibronectin-mediated adherence to endothelial cells of these streptococci was less than 25% of total and could be blocked by antifibronectin immunoglobulin G. Further treatment of endothelial cell monolayers with anti-S protein immunoglobulin G at concentrations up to 1 mg per well led to an almost complete inhibition of adherence for all tested streptococcal cultures, indicating significant contribution of S protein in the streptococcus-endothelial cell interaction. Blocking of S-protein-binding sites on streptococci by preincubation with exogeneous S protein at a concentration of 10 micrograms per 4 x 10(7) streptococci led to about 75% reduction of S-protein-mediated adherence to endothelial cells. Trypsin pretreatment of group G streptococci and pronase pretreatment of group A and G streptococci, modifications known to destroy the bacterial binding sites of S protein, also inhibited the capacity of the streptococci for S-protein-mediated adherence to endothelial cells by 75 to 80%. These results indicate that S protein plays a mediatory role in adherence of streptococci to endothelial cells and that S-protein-specific binding sites on streptococci are involved in this interaction.[1]References
- Mediation of adherence of streptococci to human endothelial cells by complement S protein (vitronectin). Valentin-Weigand, P., Grulich-Henn, J., Chhatwal, G.S., Müller-Berghaus, G., Blobel, H., Preissner, K.T. Infect. Immun. (1988) [Pubmed]
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