Abstract
Streptococcus suis causes sepsis, meningitis, and other serious infections in piglets, and meningitis in humans. Hemagglutination inhibition experiments with mono- and oligosaccharides and glycoproteins indicated that galactose-binding strains of S. suis recognized the Gal alpha 1-4Gal sequence present in the P1 and Pk blood group antigen structures. In thin-layer chromatography overlay assays the bacteria bound to trihexosylceramide (GbO3) but not to globoside (GbO4) or Forssman glycolipid (GbO5), in contrast to P-fimbriated Escherichia coli, which bound only to the latter two. The S. suis adhesin also differed from that of E. coli in that some of the hydrogen bonds formed with the receptor, as determined with chemically modified receptor analogues, were different. In agreement with the binding specificity, the S. suis bacteria agglutinated best among P blood group erythrocytes those of the P1k and P2k type, and from different animal erythrocytes those from rabbit, which express GbO3 as the predominant glycolipid. Binding to frozen sections of pig pharyngeal tissue was decreased by the free GbO3 oligosaccharide and its protein conjugate, which indicated that the corresponding glycolipid may function as receptor for galactose-binding strains of S. suis in pig pharyngeal epithelium.
Highlights
Streptococcussuis causessepsis, meningitis, and cytes by severalstrains of S. suis hasbeen found to be other serious infections in piglets, and meningitis in inhibited by galactose,whichsuggests thatthis adhesion humans
The S. suis adhesin differed from that of E. coli in that some of the hydrogen bonds formed with the receptor, as determined with chemically modified receptor analogues, were different
Increased amountsof galactose-binding strains of suis rec- Trihexosyl ceramide (GbOs) occur in the rarePIkand PZktypes of human erythrocytes, and rabbit erythrocytes have GbO3 as the predominant neutral glycolipid [15].E . coli has adhesins that bind to bthloeod the binding specificity, the S. suis bacteria agglutin- group P-related glycolipids GbO3, Gb04, and Gb05, but none ated best among P blood group erythrocytes those of that would be specificfor GbO3 [15]
Summary
628, which had the strongest and most conshtaenmtagglutination activity of the galactose-inhibitableS. The bacteria agglutinatenativeerythrocytes, sialidasecentrifugation a t 4 "C through a 5 ml layer of 6% BSA in Pi/NaCI at treated erythrocytes showed a somewhat better agglutination. For a higher specific activity (0.1 cpm/cfu), lo9streptococci were iodinated withthechloramine T method [25]using 0.5 mCi of carrier-free N a 9 in 1 ml of Pi/NaC1 and washed by centrifugations through a activity and were used routinely for the assays. Methyl a-D-galaCtOSe was a better inhibitor than methyl layer of 6% BSA. Of the disaccharides plates were coated by incubation with 100 pl of glycoprotein solution at theconcentrationsindicatedinP,/NaCI a t 23 "C for2h and washed three times with200 p1 of Pi/NaC1. Mannose, fucose, or N-acetylglucosamine (200 mM) did not inhibit hemagglutination
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