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The GALα1–4GAL-Binding Adhesin of Streptococcus Suis, A Gram-Positive Meningitis-Associated Bacterium

  • Sauli Haataja
  • Kaarina Tikkanen
  • Jukka Hytönen
  • Jukka Finne
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 408)

Summary

Streptococcus suis causes septicaemia and meningitis in pigs and occasionally in humans. A major galactose-inhibitable adhesin recognizing the blood group P -related disaccharide Galαl–4Ga1β1-present in the GbO3 glycolipid was identified in S. suis. Two variant adhesins, inhibitable by galactose and N-acetylgalactosamine (type PN) or galactose only (type PO) both preferred the disaccharide in terminal position. The hydrogen bonding patterns were determined using deoxy and other derivatives of the receptor disaccharide, and were compared to that of E. coli PapG396 adhesin. The essential hydroxyls were the HO-4’, HO-6’, HO-2 and HO-3 hydroxyls; type PO adhesin also weakly interacted with HO-6 and HO-3’. The mechanism differed from that of E. coli which binds to a cluster of five hydroxyls, HO-6, HO-2’, HO-3’, HO-4’ and HO-6’. The purified adhesin had a molecular weight of 18 kDa and an isoelectric point of 6.4. The agglutination of latex-bound purified adhesin was inhibited by the same inhibitors as agglutination with whole bacteria. The adhesin was detected by immunoblot analysis in all 23 S. suis strains examined representing different serotypes, was highly immunogenic and showed opsonizing activity. This represents the first example of the comparison of the saccharide receptor hydrogen bondings of two bacteria of different origin and shows that the same saccharide may be recognised by two different mechanisms. As a potential virulence factor present in different serotypes the adhesin represents a potential vaccine against S. suis infections.

Keywords

Sialic Acid Bacterial Meningitis Hydrogen Bond Donor Hemagglutination Inhibition Hemagglutination Activity 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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Copyright information

© Plenum Press, New York 1996

Authors and Affiliations

  • Sauli Haataja
    • 1
  • Kaarina Tikkanen
    • 2
  • Jukka Hytönen
    • 1
  • Jukka Finne
    • 1
    • 2
  1. 1.Department of Medical BiochemistryUniversity of TurkuTurkuFinland
  2. 2.Department of Biochemistry and Biotechnology A. I. Virtanen InstituteUniversity of KuopioKuopioFinland

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