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SabA is the H. pylori hemagglutinin and is polymorphic in binding to sialylated glycans

Aspholm, Marina ; Olfat, Farzad O. ; Norden, Jenny ; Sonden, Berit ; Lundberg, Carina ; Sjostrom, Rolf ; Altraja, Siiri ; Odenbreit, Stefan ; Haas, Rainer and Wadström, Torkel LU , et al. (2006) In PLoS Pathogens 2(10). p.989-1001
Abstract
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... (More)
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 NeuAc alpha 2-3Gal-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. (Less)
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organization
publishing date
type
Contribution to journal
publication status
published
subject
in
PLoS Pathogens
volume
2
issue
10
pages
989 - 1001
publisher
Public Library of Science
external identifiers
  • wos:000242786900011
  • pmid:17121461
  • scopus:33750489397
ISSN
1553-7366
DOI
10.1371/journal.ppat.0020110
language
English
LU publication?
yes
id
0ff64df6-179c-4a97-81b0-db451953d6f8 (old id 682092)
date added to LUP
2016-04-01 12:11:22
date last changed
2021-10-06 02:56:12
@article{0ff64df6-179c-4a97-81b0-db451953d6f8,
  abstract     = {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 NeuAc alpha 2-3Gal-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.},
  author       = {Aspholm, Marina and Olfat, Farzad O. and Norden, Jenny and Sonden, Berit and Lundberg, Carina and Sjostrom, Rolf and Altraja, Siiri and Odenbreit, Stefan and Haas, Rainer and Wadström, Torkel and Engstrand, Lars and Semino-Mora, Cristina and Liu, Hui and Dubois, Andre and Teneberg, Susann and Arnqvist, Anna and Boren, Thomas},
  issn         = {1553-7366},
  language     = {eng},
  number       = {10},
  pages        = {989--1001},
  publisher    = {Public Library of Science},
  series       = {PLoS Pathogens},
  title        = {SabA is the H. pylori hemagglutinin and is polymorphic in binding to sialylated glycans},
  url          = {http://dx.doi.org/10.1371/journal.ppat.0020110},
  doi          = {10.1371/journal.ppat.0020110},
  volume       = {2},
  year         = {2006},
}