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Research article

Rhesus monkey gastric mucins: oligomeric structure, glycoforms and Helicobacter pylori binding

Sara LINDÉN, Thomas BORÉN, André DUBOIS, Ingemar CARLSTEDT
Biochemical Journal May 01, 2004, 379 (3) 765-775; DOI: 10.1042/bj20031557
Sara LINDÉN
Mucosal Biology Group, Department of Cell and Molecular Biology, Biomedical Center, Lund University, SE-22184 Lund, Sweden
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Thomas BORÉN
Department of Odontology/Oral Microbiology, Umeå University, SE-90187 Umeå, Sweden
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André DUBOIS
Laboratory of Gastrointestinal and Liver Studies, Digestive Diseases Division, Department of Medicine, Uniformed Services University of the Health Sciences, Bethesda, MD, U.S.A.
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Ingemar CARLSTEDT
Mucosal Biology Group, Department of Cell and Molecular Biology, Biomedical Center, Lund University, SE-22184 Lund, Sweden
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Abstract

Mucins isolated from the stomach of Rhesus monkey are oligomeric glycoproteins with a similar mass, density, glycoform profile and tissue localization as human MUC5AC and MUC6. Antibodies raised against the human mucins recognize those from monkey, which thus appear to be orthologous to those from human beings. Rhesus monkey muc5ac and muc6 are produced by the gastric-surface epithelium and glands respectively, and occur as three distinct glycoforms. The mucins are substituted with the histo blood-group antigens B, Lea (Lewis a), Leb, Lex, Ley, H-type-2, the Tn-antigen, the T-antigen, the sialyl-Lex and sialyl-Lea structures, and the expression of these determinants varies between individuals. At neutral pH, Helicobacter pylori strains expressing BabA (blood-group antigen-binding adhesin) bind Rhesus monkey gastric mucins via the Leb or H-type-1 structures, apparently on muc5ac, as well as on a smaller putative mucin, and binding is inhibited by Leb or H-type-1 conjugates. A SabA (sialic acid-binding adhesin)-positive H. pylori mutant binds to sialyl-Lex-positive mucins to a smaller extent compared with the BabA-positive strains. At acidic pH, the microbe binds to mucins substituted by sialylated structures such as sialyl-Lex and sialylated type-2 core, and this binding is inhibited by DNA and dextran sulphate. Thus mucin–H. pylori binding occurs via at least three different mechanisms: (1) BabA-dependent binding to Leb and related structures, (2) SabA-dependent binding to sialyl-Lex and (3) binding through a charge-mediated mechanism to sialylated structures at low pH values.

  • gastric mucosa
  • glycoform
  • Helicobacter pylori
  • Lewis antigen
  • mucin
  • Rhesus monkey

Footnotes

  • ↵1 The opinions and assertions contained herein are the private ones of the authors and are not to be construed as official or reflecting the views of the Department of Defence or Uniformed Services University of the Health Sciences.

  • Abbreviations used: BabA, blood-group antigen-binding adhesin; DBA, Dolichos biflorus; HSA, human serum albumin; GdmCl, guanidinium chloride; Lea, Lewis a; MAL, Maakia amurensis II; PNA, peanut agglutinin; SabA, sialic acid-binding adhesin.

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May 2004

Volume: 379 Issue: 3

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Rhesus monkey gastric mucins: oligomeric structure, glycoforms and Helicobacter pylori binding
Sara LINDÉN, Thomas BORÉN, André DUBOIS, Ingemar CARLSTEDT
Biochemical Journal May 2004, 379 (3) 765-775; DOI: 10.1042/bj20031557
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Rhesus monkey gastric mucins: oligomeric structure, glycoforms and Helicobacter pylori binding
Sara LINDÉN, Thomas BORÉN, André DUBOIS, Ingemar CARLSTEDT
Biochemical Journal May 2004, 379 (3) 765-775; DOI: 10.1042/bj20031557

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Keywords

gastric mucosa
glycoform
Helicobacter pylori
Lewis antigen
mucin
Rhesus monkey

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