Role of cell-associated -acetyl--glucosamine specific haemagglutinin in the adhesion of O1 to rabbit intestinal epithelial cells in vitro

Sasmal, D.; Guhathakurta, B.; Bhattacharya, Shreya; Pal, Chiranjib; Datta, A.

doi:10.1016/0928-8244(95)00090-9

Cited by 9 publications

(10 citation statements)

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“…After 1.5 hours of incubation unbound proteins were washed with PBS. V. cholerae N16961O1 El Tor was biotinylated as described previously [48]. 1×10 4 CFU/ml of biotinylated V. cholerae were added to each well.…”

Section: Methodsmentioning

confidence: 99%

The Vibrio cholerae Colonization Factor GbpA Possesses a Modular Structure that Governs Binding to Different Host Surfaces

et al. 2012

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Vibrio cholerae is a bacterial pathogen that colonizes the chitinous exoskeleton of zooplankton as well as the human gastrointestinal tract. Colonization of these different niches involves an N-acetylglucosamine binding protein (GbpA) that has been reported to mediate bacterial attachment to both marine chitin and mammalian intestinal mucin through an unknown molecular mechanism. We report structural studies that reveal that GbpA possesses an unusual, elongated, four-domain structure, with domains 1 and 4 showing structural homology to chitin binding domains. A glycan screen revealed that GbpA binds to GlcNAc oligosaccharides. Structure-guided GbpA truncation mutants show that domains 1 and 4 of GbpA interact with chitin in vitro, whereas in vivo complementation studies reveal that domain 1 is also crucial for mucin binding and intestinal colonization. Bacterial binding studies show that domains 2 and 3 bind to the V. cholerae surface. Finally, mouse virulence assays show that only the first three domains of GbpA are required for colonization. These results explain how GbpA provides structural/functional modular interactions between V. cholerae, intestinal epithelium and chitinous exoskeletons.

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Section: Methodsmentioning

confidence: 99%

The Vibrio cholerae Colonization Factor GbpA Possesses a Modular Structure that Governs Binding to Different Host Surfaces

et al. 2012

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“…Bacterial ligands mediating adhesion to chitin by a specific binding to Nacetylglucosamine (GlcNAc) have been shown to be present in V. cholerae classical strains. A cellassociated GlcNAc specific hemagglutinin (HA) was purified from V. cholerae by affinity chromatography on a chitin column, followed by BioGel filtration (16). Chitin-binding proteins (CBPs) associated with the cell wall have been described by Tarsi and Pruzzo (17) and Zampini et al (18), who extended previous studies on Vibrio harveyi (19) and Vibrio alginolyticus (20), and identified two surface proteins (36 kDa and 53 kDa) involved in adhesion of V. cholerae classical strains to chitin beads and copepods.…”

Section: Cholerae á Bivalve Interactions and Link With Pathogenicitymentioning

confidence: 99%

Adhesins acquired in the aquatic environment andVibrio choleraecolonization of intestinal cells

Vezzulli

Repetto

Pezzati

et al. 2008

Microbial Ecology in Health and Disease

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Recent results for Vibrio cholerae interactions with bivalves and chitin-containing substrates are reviewed. Chitin, composed of b-1,4-linked N-acetylglucosamine residues, is one of the most abundant biopolymers in nature and the most abundant in the marine environment. V. cholerae connection to chitin is a well known phenomenon and one of the best documented examples of a successful bacteriaÁsubstrate interaction, affecting both the lifestyle of the microorganisms and natural system functioning. In sea water, vibrios can be entrapped by filter-feeding invertebrates that sieve suspended food particles from the aquatic environment. Persistence of bacteria in bivalves depends on different factors including their sensitivity to the bactericidal activity of hemolymph. Both V. cholerae survival inside bivalves and chitin colonization depend on cell surface properties, with contribution of different ligands (e.g. chitin-binding proteins, MSHA). The role of these ligands in interactions with human surfaces is discussed and evidence is presented supporting (i) the link between vibrio persistence in the environment (both inside bivalves and adhering to chitin-containing surfaces) and infection of the human host, and (ii) the hypothesis that virulence mechanisms of bacteria that have environmental reservoirs represent a consequence of adaptive mechanisms to the environment.

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“…A cell‐associated N ‐acetyl‐ d ‐glucosamine specific hemagglutinin (HA) was isolated and purified from a strain of Vibrio cholerae O1 by affinity chromatography on a chitin column followed by BioGel filtration [6]. The purified HA was documented as an adhesin molecule in V. cholerae O1 cells as studied in adhesion assays using isolated rabbit intestinal epithelial cells (RIEC) and rabbit intestinal brush borders (RIBB) in the presence of HA antisera and Fab (IgG) fragments of the HA antibody [7]. The purified HA, free from lipopolysaccharide, as evidenced by immunodiffusion and ELISA test, exhibited a single stained protein band of 47 kDa in SDS–PAGE.…”

Section: Introductionmentioning

confidence: 99%

N-Acetyl-d-glucosamine specific hemagglutinin receptor ofVibrio choleraeO1 in chicken erythrocyte membranes

Sasmal

Guhathakurta

Bhattacharya

et al. 2002

FEMS Immunology &Amp; Medical Microbiology

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N-Acetyl-D-glucosamine specific cell-associated hemagglutinin (HA)/lectin, previously purified from a strain of Vibrio cholerae O1, had been established as an adhesin molecule of V. cholerae O1 cells. This communication records the isolation and purification of the glycoprotein receptor of the N-acetyl-D-glucosamine specific HA of the V. cholerae O1 strain from chicken erythrocyte membranes. The most salient feature of this study is that the pretreatment of partially purified glycoprotein with purified HA could completely inhibit the hemagglutinating activity of the V. cholerae O1 strain with chicken erythrocytes.

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Role of cell-associated -acetyl--glucosamine specific haemagglutinin in the adhesion of O1 to rabbit intestinal epithelial cells in vitro

Cited by 9 publications

References 0 publications

The Vibrio cholerae Colonization Factor GbpA Possesses a Modular Structure that Governs Binding to Different Host Surfaces

The Vibrio cholerae Colonization Factor GbpA Possesses a Modular Structure that Governs Binding to Different Host Surfaces

Adhesins acquired in the aquatic environment andVibrio choleraecolonization of intestinal cells

N-Acetyl-d-glucosamine specific hemagglutinin receptor ofVibrio choleraeO1 in chicken erythrocyte membranes

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