Helicobacter pylori lipopolysaccharide structural domains and their recognition by immune proteins revealed with carbohydrate microarrays.
Carbohydr Polym
; 253: 117350, 2021 Feb 01.
Article
en En
| MEDLINE
| ID: mdl-33278960
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.
Palabras clave
Texto completo:
1
Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Inmunoglobulina G
/
Proteínas Sanguíneas
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Moléculas de Adhesión Celular
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Lipopolisacáridos
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Helicobacter pylori
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Infecciones por Helicobacter
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Receptores de Superficie Celular
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Lectinas Tipo C
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Galectinas
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Antígenos Bacterianos
Límite:
Adult
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Female
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Humans
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Male
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Middle aged
Idioma:
En
Revista:
Carbohydr Polym
Año:
2021
Tipo del documento:
Article
Pais de publicación:
Reino Unido