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

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

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

Marina Aspholm,Farzad O Olfat,Jenny ,Berit ,Carina Lundberg,Rolf ,Siiri Altraja,Stefan Odenbreit,Rainer Haas,Torkel ,Lars Engstrand,Cristina Semino-Mora,Hui Liu, Dubois,Susann Teneberg,Anna Arnqvist,Thomas ,

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.

SabA is the H. pylori hemagglutinin and is polymorphic in binding to sialylated glycans. Publishing Authors By Initials

M Aspholm,FO Olfat,J ,B ,C Lundberg,R ,S Altraja,S Odenbreit,R Haas,T ,L Engstrand,C Semino-Mora,H Liu,A Dubois,S Teneberg,A Arnqvist,T ,

For similar cardiovascular system: blood vessels: microcirculation: venules research abstracts see: cardiovascular system: blood vessels: microcirculation: venules research

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

PUBLICATION TYPE: Research Support, Non-U.S. Gov

Journal: PLoS pathogens

VOLUME: 2

Page Numbers: e110

Journal Abbreviation: PLoS Pathog.

ISSN: 1553-7374

DAY: 3

MONTH: Oct

YEAR: 2006

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

Number of References:

LANGUAGE: eng

NlmUniqueID: 101238921

SabA is the H. pylori hemagglutinin and is polymorphic in binding to sialylated glycans. Keywords Mesh Terms:

KEYWORDS: Venules

MESH TERMS: metabolism

Chemical & Substance for Abstract: SabA is the H. pylori hemagglutinin and is polymorphic in binding to sialylated glycans. Information

Substance Name: N-Acetylneuraminic Acid

Registry Number: 131-48-6

Grant and Affiliation Information for SabA is the H. pylori hemagglutinin and is polymorphic in binding to sialylated glycans.

AFFILIATION: Department of Odontology, Section of Oral Microbiology, Umeå University, Umeå, Sweden.

Country: United States

AGENCY: United States ADAMHA

GRANT: CA82312/AD

ACRONYM: AD

MEDLINETA: PLoS Pathog

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