Till sidans topp

Sidansvarig: Webbredaktion
Sidan uppdaterades: 2012-09-11 15:12

Tipsa en vän
Utskriftsversion

Helicobacter pylori-bindi… - Göteborgs universitet Till startsida
Webbkarta
Till innehåll Läs mer om hur kakor används på gu.se

Helicobacter pylori-binding nonacid glycosphingolipids in the human stomach

Artikel i vetenskaplig tidskrift
Författare Chunsheng Jin
Angela Barone
T. Boren
Susann Teneberg
Publicerad i Journal of Biological Chemistry
Volym 293
Nummer/häfte 44
Sidor 17248-17266
ISSN 0021-9258
Publiceringsår 2018
Publicerad vid Institutionen för biomedicin, avdelningen för medicinsk kemi och cellbiologi
Sidor 17248-17266
Språk en
Länkar dx.doi.org/10.1074/jbc.RA118.004854
Ämnesord Helicobacter pylori, mass spectrometry (MS), glycolipid structure, adhesin, carbohydrate structure, glycoconjugate, virulence factor, gastric mucosa, glycosphingolipid characterization, H, pylori BabA adhesin, Human gastric glycosphingolipids, microbial, group-related antigens, blood-group antigens, human small-intestine, sialyl-lewis-x, mass-spectrometry, duodenal mucosae, epithelial-cells, gastric tissue, lipid rafts, adhesin, Biochemistry & Molecular Biology
Ämneskategorier Biomedicinsk laboratorievetenskap/teknologi

Sammanfattning

Helicobacter pylori has a number of well-characterized carbohydrate-binding adhesins (BabA, SabA, and LabA) that promote adhesion to the gastric mucosa. In contrast, information on the glycoconjugates present in the human stomach remains unavailable. Here, we used MS and binding of carbohydrate-recognizing ligands to characterize the glycosphingolipids of three human stomachs from individuals with different blood group phenotypes (O(Rh-)P, A(Rh+)P, and A(Rh+)p), focusing on compounds recognized by H. pylori. We observed a high degree of structural complexity, and the composition of glycosphingolipids differed among individuals with different blood groups. The type 2 chain was the dominating core chain of the complex glycosphingolipids in the human stomach, in contrast to the complex glycosphingolipids in the human small intestine, which have mainly a type 1 core. H. pylori did not bind to the O(Rh-)P stomach glycosphingolipids, whose major complex glycosphingolipids were neolactotetraosylceramide, the Le(x), Le(a), and H type 2 pentaosylceramides, and the Le(y) hexaosylceramide. Several H. pylori-binding compounds were present among the A(Rh+)P and A(Rh+)p stomach glycosphingolipids. Ligands for BabA-mediated binding of H. pylori were the Le(b) hexaosylceramide, the H type 1 pentaosylceramide, and the A type 1/ALe(b) heptaosylceramide. Additional H. pylori-binding glycosphingolipids recognized by BabA-deficient strains were lactosylceramide, lactotetraosylceramide, the x(2) pentaosylceramide, and neolactohexaosylceramide. Our characterization of human gastric receptors required for H. pylori adhesion provides a basis for the development of specific compounds that inhibit the binding of this bacterium to the human gastric mucosa.

Sidansvarig: Webbredaktion|Sidan uppdaterades: 2012-09-11
Dela:

På Göteborgs universitet använder vi kakor (cookies) för att webbplatsen ska fungera på ett bra sätt för dig. Genom att surfa vidare godkänner du att vi använder kakor.  Vad är kakor?