Helicobacter pylori lipopolysaccharide structural domains and their recognition by immune proteins revealed with carbohydrate microarrays
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Author(s)
Type
Journal Article
Abstract
The structural diversity of the lipopolysaccharides (LPSs) from Helicobacter pylori poses a challenge to establish accurate and strain-specific structure-function relationships in interactions with the host. Here, LPS structural domains from five clinical isolates were obtained and compared with the reference strain 26695. This was achieved combining information from structural analysis (GC-MS and ESI-MSn) with binding data after interrogation of a LPS-derived carbohydrate microarray with sequence-specific proteins. All LPSs expressed Lewisx/y and N-acetyllactosamine determinants. Ribans were also detected in LPSs from all clinical isolates, allowing their distinction from the 26695 LPS. There was evidence for 1,3-d-galactans and blood group H-type 2 sequences in two of the clinical isolates, the latter not yet described for H. pylori LPS. Furthermore, carbohydrate microarray analyses showed a strain-associated LPS recognition by the immune lectins DC-SIGN and galectin-3 and revealed distinctive LPS binding patterns by IgG antibodies in the serum from H. pylori-infected patients.
Date Issued
2021-02-01
Online Publication Date
2020-12-18T15:49:09Z
Date Acceptance
2020-10-29
ISSN
0144-8617
Publisher
Elsevier BV
Journal / Book Title
Carbohydrate Polymers
Volume
253
Copyright Statement
© 2020 The Authors. Published by Elsevier Ltd. This is an open access article under the CC BY license (http://creativecommons.org/licenses/by/4.0/).
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Subjects
Carbohydrate microarrays
Helicobacter pylori
Host immune receptors
Human sera
Lipopolysaccharides
Mass spectrometry
Polymers
0303 Macromolecular and Materials Chemistry
0305 Organic Chemistry
0908 Food Sciences
Publication Status
Published
Article Number
ARTN 117350
Date Publish Online
2020-11-02