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Identification of a carbohydrate receptor recognized by uropathogenic Escherichia coli

Identifizierung eines Kohlenhydratrezeptors für uropathogene Escherichia coli

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Zusammenfassung

Frühere Untersuchungen haben gezeigt. daßEscherichia coli, die Erreger von Pyelonephritis sind, Kohlenhydratstrukturen, die mit den P-Blutgruppen-Antigenen in Beziehung stehen, spezifisch erkennen und sich an sie binden. Diese Ergebnisse werden in der vorliegenden Untersuchung bestätigt und erweitert. Zweiundzwanzig von 23 nicht selektiertenE. coli-Stämmen von Kindern mit akuter fieberhafter Pyelonephritis agglutinierten menschliche Erythrozyten nicht, bei denen Antigene im P-Blutgruppensystem fehlten. Nur eines von 32 Isolaten aus dem Stuhl zeigte diese spezifische agglutinierende Eigenschaft. Die neue Information aus dieser Arbeit ist, daß P K2 -Erythrozyten, die das PK-Antigen enthielten, im selben Ausmaß vonE. coli-Stämmen, die Pyelonephritis-Erreger waren, agglutiniert wurden, womit sich die Vorstellung weiter bestärkt, daß das PK-Glykosphingolipid dem Rezeptor für PyelonephritisE. coli verwandt ist. Daneben wurde der Bedeutung der Oligosaccharid-verbindung des PK-Glykosphingolipids für die Bindung vonE. coli weiter nachgeforscht. Das synthetisierte Disaccharid α-D-Galp-(1–4)-β-D-Galp-1-O-Ø-NO2 hemmt die durch pyelonephritischeE. coli verursachte Agglutination von menschlichen Erythrozyten bei Konzentrationen von weniger als 1 mM. Folglich scheint die kleinste von diesenE. coli-Stämmen erkennbare Struktur das α-D-Galp-(1–4)-β-D-Galp zu sein. Wieweit diese Beobachtung allgemeine Bedeutung besitzt, bedarf weiterer Forschung. Die Ergebnisse können neue Möglichkeiten für die Diagnose und die Behandlung der Harnwegsinfektionen eröffnen.

Summary

Earlier investigations have shown that pyelonephriticEscherichia coli specifically recognize and bind to carbohydrate structures correlated to the P blood group antigens. These findings are confirmed and extended in this study. Twenty-two of 23 nonselectedE. coli strains from children with acute febrile pyelonephritis failed to agglutinate human erythrocytes lacking the antigens within the P blood group system. Only one of 32 faecal isolates exhibited this specific agglutinating property. The new information in this paper is that P k2 erythrocytes, containing only the Pk antigen, were agglutinated to the same extent by pyelonephriticE. coli strains, giving further support to the proposal that the Pk glycosphingolipid is related to the receptor for pyelonephriticE. coli. In addition, the importance of the oligosaccharide moiety of the Pk glycosphingolipid for the binding ofE. coli was further investigated. The synthesized disaccharide α-D-Galp-(1–4)-β-D-Galp-1-O-Ø-NO2 inhibited the agglutination of human erythrocytes caused by two pyelonephriticE. coli strains at concentrations of less than 1 mM. Hence, the minimal receptor structure recognized by theseE. coli strains appears to be the α-D-Galp-(1–4)-β-D-Galp structure. How generally valid this observation may be needs further investigation. The findings may open new possibilities for diagnosis and treatment of urinary tract infection.

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Authors and Affiliations

  1. Department of Pediatrics, Karolinska Hospital, Karolinska Institute, S-104 01, Stockholm, Sweden

    G. Källenius & J. Winberg

  2. Department of Bacteriology, National Bacteriological Laboratory, S-105 21, Stockholm, Sweden

    R. Möllby & S. B. Svenson

  3. Department of Organic Chemistry Arrhenius Laboratory, University of Stockholm, S-106 91, Stockholm, Sweden

    H. Hultberg

Authors
  1. G. Källenius
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  2. J. Winberg
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  3. R. Möllby
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  4. S. B. Svenson
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  5. H. Hultberg
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Källenius, G., Winberg, J., Möllby, R. et al. Identification of a carbohydrate receptor recognized by uropathogenic Escherichia coli. Infection 8 (Suppl 3), S288–S293 (1980). https://doi.org/10.1007/BF01639597

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