Please use this identifier to cite or link to this item: http://hdl.handle.net/10773/29891
Title: Helicobacter pylori lipopolysaccharide structural domains and their recognition by immune proteins revealed with carbohydrate microarrays
Author: Silva, Lisete M.
Correia, Viviana G.
Moreira, Ana S.P.
Domingues, Maria Rosário M.
Ferreira, Rui M.
Figueiredo, Céu
Azevedo, Nuno F.
Marcos-Pinto, Ricardo
Carneiro, Fátima
Magalhães, Ana
Reis, Celso A.
Feizi, Ten
Ferreira, José A.
Coimbra, Manuel A.
Palma, Angelina S.
Keywords: Helicobacter pylori
Lipopolysaccharides
Mass spectrometry
Carbohydrate microarrays
Host immune receptors
Human sera
Issue Date: 2020
Publisher: Elsevier
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.
Peer review: yes
URI: http://hdl.handle.net/10773/29891
DOI: 10.1016/j.carbpol.2020.117350
ISSN: 0144-8617
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