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

Lindén, Sara LU ; Boren, T; Dubois, A and Carlstedt, Ingemar LU (2004) In Biochemical Journal 379(3). p.765-775
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, Le(a) (Lewis a), Le(b), Le(x), Le(y), H-type-2, the Tn-antigen, the T-antigen, the sialyi-Le(x) and sialyi-Le(a) structures, and the expression of these determinants varies between individuals. At neutral pH, Helicobacter pylori... (More)
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, Le(a) (Lewis a), Le(b), Le(x), Le(y), H-type-2, the Tn-antigen, the T-antigen, the sialyi-Le(x) and sialyi-Le(a) 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 Le(b) or H-type-1 structures, apparently on muc5ac, as well as on a smaller putative mucin, and binding is inhibited by Le(b) or H-type-I conjugates. A SabA (sialic acid-binding adhesin)-positive H. pylori mutant binds to sialyi-Le(x)-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 sialyi-Le(x) 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 Le(b) and related structures, (2) SabA-dependent binding to sialyl-Le(x) and (3) binding through a charge-mediated mechanism to sialylated structures at low pH values. (Less)
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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
Rhesus monkey, mucin, Lewis antigen, Helicobacter pylori, gastric mucosa, glycoform
in
Biochemical Journal
volume
379
issue
3
pages
765 - 775
publisher
Portland Press Limited
external identifiers
  • wos:000221535000029
  • pmid:14736333
  • scopus:2542518445
ISSN
0264-6021
DOI
10.1042/BJ20031557
language
English
LU publication?
yes
id
fc24525e-771c-483a-a41a-d088faa9c67e (old id 277402)
date added to LUP
2007-10-24 19:17:44
date last changed
2017-04-23 04:25:27
@article{fc24525e-771c-483a-a41a-d088faa9c67e,
  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, Le(a) (Lewis a), Le(b), Le(x), Le(y), H-type-2, the Tn-antigen, the T-antigen, the sialyi-Le(x) and sialyi-Le(a) 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 Le(b) or H-type-1 structures, apparently on muc5ac, as well as on a smaller putative mucin, and binding is inhibited by Le(b) or H-type-I conjugates. A SabA (sialic acid-binding adhesin)-positive H. pylori mutant binds to sialyi-Le(x)-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 sialyi-Le(x) 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 Le(b) and related structures, (2) SabA-dependent binding to sialyl-Le(x) and (3) binding through a charge-mediated mechanism to sialylated structures at low pH values.},
  author       = {Lindén, Sara and Boren, T and Dubois, A and Carlstedt, Ingemar},
  issn         = {0264-6021},
  keyword      = {Rhesus monkey,mucin,Lewis antigen,Helicobacter pylori,gastric mucosa,glycoform},
  language     = {eng},
  number       = {3},
  pages        = {765--775},
  publisher    = {Portland Press Limited},
  series       = {Biochemical Journal},
  title        = {Rhesus monkey gastric mucins: oligomeric structure, glycoforms and Helicobacter pylori binding},
  url          = {http://dx.doi.org/10.1042/BJ20031557},
  volume       = {379},
  year         = {2004},
}