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Redefinition of the carbohydrate binding specificity of Helicobacter pylori BabA adhesin.


ABSTRACT: Certain Helicobacter pylori strains adhere to the human gastric epithelium using the blood group antigen-binding adhesin (BabA). All BabA-expressing H. pylori strains bind to the blood group O determinants on type 1 core chains, i.e. to the Lewis b antigen (Fuc?2Gal?3(Fuc?4)GlcNAc; Le(b)) and the H type 1 determinant (Fuc?2Gal?3GlcNAc). Recently, BabA strains have been categorized into those recognizing only Le(b) and H type 1 determinants (designated specialist strains) and those that also bind to A and B type 1 determinants (designated generalist strains). Here, the structural requirements for carbohydrate recognition by generalist and specialist BabA were further explored by binding of these types of strains to a panel of different glycosphingolipids. Three glycosphingolipids recognized by both specialist and generalist BabA were isolated from the small intestine of a blood group O pig and characterized by mass spectrometry and proton NMR as H type 1 pentaglycosylceramide (Fuc?2Gal?3GlcNAc?3Gal?4Glc?1Cer), Globo H hexaglycosylceramide (Fuc?2Gal?3GalNAc?3Gal?4Gal?4Glc?1Cer), and a mixture of three complex glycosphingolipids (Fuc?2Gal?4GlcNAc?6(Fuc?2Gal?3GlcNAc?3)Gal?3GlcNAc?3Gal?4Glc?1Cer, Fuc?2Gal?3GlcNAc?6(Fuc?2Gal?3GlcNAc?3)Gal?3GlcNAc?3Gal?4Glc?1Cer, and Fuc?2Gal?4(Fuc?3)GlcNAc?6(Fuc?2Gal?3GlcNAc?3)Gal?3GlcNAc?3Gal?4Glc?1Cer). In addition to the binding of both strains to the Globo H hexaglycosylceramide, i.e. a blood group O determinant on a type 4 core chain, the generalist strain bound to the Globo A heptaglycosylceramide (GalNAc?3(Fuc?2)Gal?3GalNAc?3Gal?4Gal?4Glc?1Cer), i.e. a blood group A determinant on a type 4 core chain. The binding of BabA to the two sets of isoreceptors is due to conformational similarities of the terminal disaccharides of H type 1 and Globo H and of the terminal trisaccharides of A type 1 and Globo A.

SUBMITTER: Benktander J 

PROVIDER: S-EPMC3442506 | biostudies-literature | 2012 Sep

REPOSITORIES: biostudies-literature

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Redefinition of the carbohydrate binding specificity of Helicobacter pylori BabA adhesin.

Benktander John J   Ångström Jonas J   Breimer Michael E ME   Teneberg Susann S  

The Journal of biological chemistry 20120720 38


Certain Helicobacter pylori strains adhere to the human gastric epithelium using the blood group antigen-binding adhesin (BabA). All BabA-expressing H. pylori strains bind to the blood group O determinants on type 1 core chains, i.e. to the Lewis b antigen (Fucα2Galβ3(Fucα4)GlcNAc; Le(b)) and the H type 1 determinant (Fucα2Galβ3GlcNAc). Recently, BabA strains have been categorized into those recognizing only Le(b) and H type 1 determinants (designated specialist strains) and those that also bind  ...[more]

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