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  • Adhesins, Bacterial/chemistry/genetics/isolation & purification/*metabolism  (1)
  • Bacterial Adhesion  (1)
  • 1
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    Helicobacter pylori SabA adhesin in persistent infection and chronic inflammation (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-07-27
    Description: Helicobacter pylori adherence in the human gastric mucosa involves specific bacterial adhesins and cognate host receptors. Here, we identify sialyl-dimeric-Lewis x glycosphingolipid as a receptor for H. pylori and show that H. pylori infection induced formation of sialyl-Lewis x antigens in gastric epithelium in humans and in a Rhesus monkey. The corresponding sialic acid-binding adhesin (SabA) was isolated with the "retagging" method, and the underlying sabA gene (JHP662/HP0725) was identified. The ability of many H. pylori strains to adhere to sialylated glycoconjugates expressed during chronic inflammation might thus contribute to virulence and the extraordinary chronicity of H. pylori infection.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2570540/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2570540/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Mahdavi, Jafar -- Sonden, Berit -- Hurtig, Marina -- Olfat, Farzad O -- Forsberg, Lina -- Roche, Niamh -- Angstrom, Jonas -- Larsson, Thomas -- Teneberg, Susann -- Karlsson, Karl-Anders -- Altraja, Siiri -- Wadstrom, Torkel -- Kersulyte, Dangeruta -- Berg, Douglas E -- Dubois, Andre -- Petersson, Christoffer -- Magnusson, Karl-Eric -- Norberg, Thomas -- Lindh, Frank -- Lundskog, Bertil B -- Arnqvist, Anna -- Hammarstrom, Lennart -- Boren, Thomas -- P30 DK52574/DK/NIDDK NIH HHS/ -- R01 AI38166/AI/NIAID NIH HHS/ -- R01 CA082312/CA/NCI NIH HHS/ -- R01 CA082312-08/CA/NCI NIH HHS/ -- R01 DK53727/DK/NIDDK NIH HHS/ -- R03 AI49161/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 2002 Jul 26;297(5581):573-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Odontology/Oral Microbiology, Umea University, SE-901 87 Umea, Sweden.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12142529" target="_blank"〉PubMed〈/a〉
    Keywords: Adhesins, Bacterial/chemistry/genetics/isolation & purification/*metabolism ; Amino Acid Sequence ; Animals ; Antigens, CD15/*metabolism ; *Bacterial Adhesion ; Carbohydrate Sequence ; Carrier Proteins/genetics/metabolism ; Gastric Mucosa/immunology/metabolism/*microbiology ; Gastritis/immunology/metabolism/*microbiology ; Genes, Bacterial ; Glycoconjugates/metabolism ; Helicobacter Infections/immunology/metabolism/*microbiology ; Helicobacter pylori/genetics/isolation & purification/*physiology ; Humans ; Macaca mulatta ; Mice ; Mice, Transgenic ; Molecular Sequence Data ; Oligosaccharides/*metabolism ; Sialic Acids/metabolism
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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  • 2
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    Helicobacter pylori adhesin binding fucosylated histo-blood group antigens revealed by retagging (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-02-07
    Description: The bacterium Helicobacter pylori is the causative agent for peptic ulcer disease. Bacterial adherence to the human gastric epithelial lining is mediated by the fucosylated Lewis b (Leb) histo-blood group antigen. The Leb-binding adhesin, BabA, was purified by receptor activity-directed affinity tagging. The bacterial Leb-binding phenotype was associated with the presence of the cag pathogenicity island among clinical isolates of H. pylori. A vaccine strategy based on the BabA adhesin might serve as a means to target the virulent type I strains of H. pylori.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ilver, D -- Arnqvist, A -- Ogren, J -- Frick, I M -- Kersulyte, D -- Incecik, E T -- Berg, D E -- Covacci, A -- Engstrand, L -- Boren, T -- New York, N.Y. -- Science. 1998 Jan 16;279(5349):373-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Microbiology, Umea University, SE-901 87 Umea, Sweden.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9430586" target="_blank"〉PubMed〈/a〉
    Keywords: Adhesins, Bacterial/chemistry/genetics/*isolation & purification/metabolism ; Amino Acid Sequence ; *Antigens, Bacterial ; Bacterial Adhesion ; Bacterial Proteins/genetics/physiology ; Base Composition ; Base Sequence ; Biotinylation ; Cell Membrane/chemistry ; Cloning, Molecular ; Codon, Initiator ; Fucose ; Gastric Mucosa/microbiology ; Genes, Bacterial ; Glycoconjugates/metabolism ; Helicobacter pylori/isolation & purification/*metabolism/pathogenicity ; Humans ; Lewis Blood-Group System/*metabolism ; Ligands ; Molecular Sequence Data ; Virulence
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    PAPER CURRENT
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