Abstract
Streptococcus suis is a common cause of sepsis, meningitis, and other serious infections in young piglets and also causes meningitis in humans. The cell-binding specificity of sialic acid-recognizing strains of Streptococcus suis was investigated. Treatment of human erythrocytes with sialidase or mild periodate abolished hemagglutination. Hemagglutination inhibition experiments with sialyl oligosaccharides indicated that the adhesin preferred the sequence NeuNAc alpha 2-3Gal beta 1-4Glc(NAc). Resialylation of desialylated erythrocytes with Gal beta 1-3(4)GlcNAc alpha 2-3-sialyltransferase induced a strong hemagglutination, whereas no or only weak hemagglutination was obtained with cells resialylated with two other sialyltransferases. Binding of radiolabeled bacteria to blots of erythrocyte membrane proteins revealed binding to the poly-N-acetyllactosamine-containing components Band 3, Band 4.5, and polyglycosyl ceramides and to glycophorin A. The involvement of glycophorin A as a major ligand was excluded by the strong hemagglutination of trypsin-treated erythrocytes and En(a-) erythrocytes defective in glycophorin A. Sensitivity of the hemagglutination toward endo-beta-galactosidase treatment of erythrocytes and inhibition by purified poly-N-acetyllactosaminyl glycopeptides indicated that the adhesin bound to glycans containing the following structure: NeuNAc alpha 2-3Gal beta 1-4GlcNAc beta 1-3Gal beta 1-.
Highlights
Streptococcus suis is a common cause of sepsis, men- protein oligosaccharides have been reported only in few cases ingitis, and other serious infections in young piglets [8,9]
Hemagglutination of Resialyluted Erythrocytes-Erythrosuspension in Pi/NaCl corresponding to four times the agglutination cytes resialylated with sialyltransferases were used before to titer were pipetted onto aceramic ring glass slide and kept on ice for characterize the binding activity of sialic acid-binding E. coli
Since thepotential glycoprotein and glycolipid acceptors of this sialyltransferase contain galactose 81-4 but not 81-3 linked to N-acetyglucosamine [33, 34], the results suggest that the S. suis strains bind to NeuNAca2-3Ga1/31-4GlcNAc containing molecules of the erythrocyte membrane
Summary
Resialylation of sialidase-treated erythrocytes was carried out as Sialic Acid Specificity of Hemagglutination-Similar to S-. Hemagglutination of Resialyluted Erythrocytes-Erythrosuspension in Pi/NaCl corresponding to four times the agglutination cytes resialylated with sialyltransferases were used before to titer were pipetted onto aceramic ring glass slide and kept on ice for characterize the binding activity of sialic acid-binding E. coli. After sodium dodecyl sulfate-electrophoresis in 8%polyacrylamidegels [22] and blotting to nitrocellulose the S. suis strains, erythrocytes treated with sialidase were resialylated withGalpl-3GalNAc a2-3-sialyltransferase, Galpl-4GlcNAc a2-6-sialyltransferase, or Galpl-3(4)GlcNAc a2-3-sialyltransferase. To a specific activity of 0.02 cpmfiacterium, treated cells was lower than in the other cells (Table 11), a separateexperimentwith higher incorporation (upto 53 nmol/ml) did not show increase in agglutination with this and the blots were incubated without shaking with 10' labeled bacteria/ml in PJNaCl containing 2% albumin at 23 "C for 2 h. Effect of different treatments of erythrocytes on hemagglutination induced by 5'. suis strains B147 and KU5
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