SabA is the H. pylori hemagglutinin and is polymorphic in binding to sialylated glycans.
Adherence of Helicobacter pylori to inflamed gastric mucosa is dependent on the sialic acid-binding adhesin (SabA) and cognate sialylated/fucosylated glycans on the host cell surface. By in situ hybridization, H. pylori bacteria were observed in close association with erythrocytes in capillaries and...
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2006-10-01
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doaj-c629c2ba3cda44de8d0183f4a6ef637e2020-11-25T01:58:25ZengPublic Library of Science (PLoS)PLoS Pathogens1553-73661553-73742006-10-01210e11010.1371/journal.ppat.0020110SabA is the H. pylori hemagglutinin and is polymorphic in binding to sialylated glycans.Marina AspholmFarzad O OlfatJenny NordénBerit SondénCarina LundbergRolf SjöströmSiiri AltrajaStefan OdenbreitRainer HaasTorkel WadströmLars EngstrandCristina Semino-MoraHui LiuAndré DuboisSusann TenebergAnna ArnqvistThomas BorénAdherence of Helicobacter pylori to inflamed gastric mucosa is dependent on the sialic acid-binding adhesin (SabA) and cognate sialylated/fucosylated glycans on the host cell surface. By in situ hybridization, H. pylori bacteria were observed in close association with erythrocytes in capillaries and post-capillary venules of the lamina propria of gastric mucosa in both infected humans and Rhesus monkeys. In vivo adherence of H. pylori to erythrocytes may require molecular mechanisms similar to the sialic acid-dependent in vitro agglutination of erythrocytes (i.e., sialic acid-dependent hemagglutination). In this context, the SabA adhesin was identified as the sialic acid-dependent hemagglutinin based on sialidase-sensitive hemagglutination, binding assays with sialylated glycoconjugates, and analysis of a series of isogenic sabA deletion mutants. The topographic presentation of binding sites for SabA on the erythrocyte membrane was mapped to gangliosides with extended core chains. However, receptor mapping revealed that the NeuAcalpha2-3Gal-disaccharide constitutes the minimal sialylated binding epitope required for SabA binding. Furthermore, clinical isolates demonstrated polymorphism in sialyl binding and complementation analysis of sabA mutants demonstrated that polymorphism in sialyl binding is an inherent property of the SabA protein itself. Gastric inflammation is associated with periodic changes in the composition of mucosal sialylation patterns. We suggest that dynamic adaptation in sialyl-binding properties during persistent infection specializes H. pylori both for individual variation in mucosal glycosylation and tropism for local areas of inflamed and/or dysplastic tissue.http://europepmc.org/articles/PMC1626103?pdf=render |
collection |
DOAJ |
language |
English |
format |
Article |
sources |
DOAJ |
author |
Marina Aspholm Farzad O Olfat Jenny Nordén Berit Sondén Carina Lundberg Rolf Sjöström Siiri Altraja Stefan Odenbreit Rainer Haas Torkel Wadström Lars Engstrand Cristina Semino-Mora Hui Liu André Dubois Susann Teneberg Anna Arnqvist Thomas Borén |
spellingShingle |
Marina Aspholm Farzad O Olfat Jenny Nordén Berit Sondén Carina Lundberg Rolf Sjöström Siiri Altraja Stefan Odenbreit Rainer Haas Torkel Wadström Lars Engstrand Cristina Semino-Mora Hui Liu André Dubois Susann Teneberg Anna Arnqvist Thomas Borén SabA is the H. pylori hemagglutinin and is polymorphic in binding to sialylated glycans. PLoS Pathogens |
author_facet |
Marina Aspholm Farzad O Olfat Jenny Nordén Berit Sondén Carina Lundberg Rolf Sjöström Siiri Altraja Stefan Odenbreit Rainer Haas Torkel Wadström Lars Engstrand Cristina Semino-Mora Hui Liu André Dubois Susann Teneberg Anna Arnqvist Thomas Borén |
author_sort |
Marina Aspholm |
title |
SabA is the H. pylori hemagglutinin and is polymorphic in binding to sialylated glycans. |
title_short |
SabA is the H. pylori hemagglutinin and is polymorphic in binding to sialylated glycans. |
title_full |
SabA is the H. pylori hemagglutinin and is polymorphic in binding to sialylated glycans. |
title_fullStr |
SabA is the H. pylori hemagglutinin and is polymorphic in binding to sialylated glycans. |
title_full_unstemmed |
SabA is the H. pylori hemagglutinin and is polymorphic in binding to sialylated glycans. |
title_sort |
saba is the h. pylori hemagglutinin and is polymorphic in binding to sialylated glycans. |
publisher |
Public Library of Science (PLoS) |
series |
PLoS Pathogens |
issn |
1553-7366 1553-7374 |
publishDate |
2006-10-01 |
description |
Adherence of Helicobacter pylori to inflamed gastric mucosa is dependent on the sialic acid-binding adhesin (SabA) and cognate sialylated/fucosylated glycans on the host cell surface. By in situ hybridization, H. pylori bacteria were observed in close association with erythrocytes in capillaries and post-capillary venules of the lamina propria of gastric mucosa in both infected humans and Rhesus monkeys. In vivo adherence of H. pylori to erythrocytes may require molecular mechanisms similar to the sialic acid-dependent in vitro agglutination of erythrocytes (i.e., sialic acid-dependent hemagglutination). In this context, the SabA adhesin was identified as the sialic acid-dependent hemagglutinin based on sialidase-sensitive hemagglutination, binding assays with sialylated glycoconjugates, and analysis of a series of isogenic sabA deletion mutants. The topographic presentation of binding sites for SabA on the erythrocyte membrane was mapped to gangliosides with extended core chains. However, receptor mapping revealed that the NeuAcalpha2-3Gal-disaccharide constitutes the minimal sialylated binding epitope required for SabA binding. Furthermore, clinical isolates demonstrated polymorphism in sialyl binding and complementation analysis of sabA mutants demonstrated that polymorphism in sialyl binding is an inherent property of the SabA protein itself. Gastric inflammation is associated with periodic changes in the composition of mucosal sialylation patterns. We suggest that dynamic adaptation in sialyl-binding properties during persistent infection specializes H. pylori both for individual variation in mucosal glycosylation and tropism for local areas of inflamed and/or dysplastic tissue. |
url |
http://europepmc.org/articles/PMC1626103?pdf=render |
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