Characterization of moose intestinal glycosphingolipids

Johansson, Miralda Madar; Dedic, Benjamin; Lundholm, Klara; Branzell, Filip Berner; Barone, Angela; Benktander, John; Teneberg, Susann

doi:10.1007/s10719-015-9604-8

Cited by 13 publications

(12 citation statements)

References 43 publications

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“…The native nonacid glycosphingolipid fractions were analyzed by LC-ESI/MS as described (56). Aliquots of the glycosphingolipid fractions were dissolved in methanol/acetonitrile (75:25 by volume) and separated on a 100 ϫ 0.250-mm column, packed in-house with 5-m polyamine II particles (YMC Europe GmbH, Dinslaken, Germany).…”

Section: Lc-esi/ms Of Native Glycosphingolipidsmentioning

confidence: 99%

Helicobacter pylori–binding nonacid glycosphingolipids in the human stomach

Jin

Barone

Borén

et al. 2018

Journal of Biological Chemistry

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Edited by Chris WhitfieldHelicobacter 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 carbohydraterecognizing 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.

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Section: Lc-esi/ms Of Native Glycosphingolipidsmentioning

confidence: 99%

Helicobacter pylori–binding nonacid glycosphingolipids in the human stomach

Jin

Barone

Borén

et al. 2018

Journal of Biological Chemistry

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“…LC-ESI/MS of the native acid glycosphingolipids was done as described [ 53 ]. The glycosphingolipids were dissolved in methanol:acetonitrile in proportion 75:25 (by volume) and separated on a 200 × 0.150 mm column, packed in-house with 5 μm polyamine II particles (YMC Europe GmbH; PB12S05).…”

Section: Methodsmentioning

confidence: 99%

Helicobacter pylori SabA binding gangliosides of human stomach

et al. 2018

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Adhesion of Helicobacter pylori to the gastric mucosa is a prerequisite for the pathogenesis of H. pylori related diseases. In this study, we investigated the ganglioside composition of human stomach as the target for attachment mediated by H. pylori SabA (sialic acid binding adhesin). Acid glycosphingolipids were isolated from human stomach and separated into subfractions, which were characterized by mass spectrometry and by binding of antibodies, bacteria, and Solanum tuberosum lectin. H. pylori SabA binding gangliosides were characterized as Neu5Acα3-neolactohexaosylceramide and Neu5Acα3-neolactooctaosylceramide, while the other acid human stomach glycosphingolipids characterized (sulfatide and the gangliosides GM3, GD3, GM1, Neu5Acα3-neolactotetraosylceramide, GD1a and GD1b) were not recognized by the bacteria. Defining H. pylori binding glycosphingolipids of the human gastric mucosa will be useful to specifically target this microbe-host interaction for therapeutic intervention.

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“…Native glycosphingolipids were analyzed by LC-ESI/MS as described (44). Glycosphingolipids were dissolved in methanol:acetonitrile in proportion 75:25 (by volume) and separated on a 200x0.150 mm column, packed in-house with 5 µM polyamine II particles (YMC Europe GmbH, Dinslaken, Germany).…”

Section: Lc-esi/ms Of Native Glycosphingolipidsmentioning

confidence: 99%

The binding mechanism of the virulence factor Streptococcus suis adhesin P subtype to globotetraosylceramide is associated with systemic disease

Johansson

Bélurier

Papageorgiou

et al. 2020

Journal of Biological Chemistry

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Streptococcus suis is part of the pig commensal microbiome but strains can also be pathogenic, causing pneumonia and meningitis in pigs as well as zoonotic meningitis. According to genomic analysis, S. suis is divided into asymptomatic carriage, respiratory and systemic strains with distinct genomic signatures. Since the strategies to target pathogenic S. suis are limited, new therapeutic approaches are needed. The virulence factor S. suis adhesin P (SadP) recognizes the galabiose Galα1–4Gal-oligosaccharide. Based on its oligosaccharide fine specificity, SadP can be divided into subtypes PN and PO. We show here that subtype PN is distributed in the systemic strains causing meningitis, whereas type PO is found in asymptomatic carriage and respiratory strains. Both types of SadP are shown to predominantly bind to pig lung globotriaosylceramide (Gb3). However, SadP adhesin from systemic subtype PN strains also binds to globotetraosylceramide (Gb4). Mutagenesis studies of the galabiose-binding domain of type PN SadP adhesin showed that the amino acid asparagine-285, which is replaced by an aspartate residue in type PO SadP, was required for binding to Gb4 and, strikingly, was also required for interaction with the glycomimetic inhibitor phenylurea-galabiose. Molecular dynamics simulations provided insight into the role of Asn-285 for Gb4 and phenylurea-galabiose binding, suggesting additional hydrogen bonding to terminal GalNAc of Gb4 and urea-group. Thus, the Asn-285-mediated molecular mechanism of type PN SadP binding to Gb4 could be used to selectively target S. suis in systemic disease without interfering with commensal strains, opening up new avenues for interventional strategies against this pathogen.

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Characterization of moose intestinal glycosphingolipids

Cited by 13 publications

References 43 publications

Helicobacter pylori–binding nonacid glycosphingolipids in the human stomach

Helicobacter pylori–binding nonacid glycosphingolipids in the human stomach

Helicobacter pylori SabA binding gangliosides of human stomach

The binding mechanism of the virulence factor Streptococcus suis adhesin P subtype to globotetraosylceramide is associated with systemic disease

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