Recognition of the blood group H type 2 trisaccharide epitope by 28 monoclonal antibodies and three lectins

Mollicone, Rosella; Cailleau, Anne; Imberty, Anne; Gane, Pierre; Pérez, Serge; Oriol, Rafaël

doi:10.1007/bf00731501

Cited by 34 publications

(21 citation statements)

References 36 publications

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“…3E), suggesting that the existence of Fucα1-2Gal disaccharide unit. The observed low binding of Globo H is consistent with the previous data showing that the lectin UEA-1 is unreactive to the H-type 3/4 structures (40,41). Taken together, the results provide evidence that our Reishi polysaccharides contain α-Lfucosylated glycans but may differ from the Globo H-series structures.…”

Section: Fuc-enriched F3 Polysaccharide Fraction Induced Antibodies Rsupporting

confidence: 91%

Immunization of fucose-containing polysaccharides from Reishi mushroom induces antibodies to tumor-associated Globo H-series epitopes

Liao

Liang

et al. 2013

Proc. Natl. Acad. Sci. U.S.A.

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Carbohydrate-based vaccines have shown therapeutic efficacy for infectious disease and cancer. The mushroom Ganoderma lucidum (Reishi) containing complex polysaccharides has been used as antitumor supplement, but the mechanism of immune response has rarely been studied. Here, we show that the mice immunized with a L-fucose (Fuc)-enriched Reishi polysaccharide fraction (designated as FMS) induce antibodies against murine Lewis lung carcinoma cells, with increased antibody-mediated cytotoxicity and reduced production of tumor-associated inflammatory mediators (in particular, monocyte chemoattractant protein-1). The mice showed a significant increase in the peritoneal B1 B-cell population, suggesting FMS-mediated anti-glycan IgM production. Furthermore, the glycan microarray analysis of FMS-induced antisera displayed a high specificity toward tumor-associated glycans, with the antigenic structure located in the nonreducing termini (i.e., Fucα1-2Galβ1-3GalNAc-R, where Gal, GalNAc, and R represent, respectively, Dgalactose, D-N-acetyl galactosamine, and reducing end), typically found in Globo H and related tumor antigens. The composition of FMS contains mainly the backbone of 1,4-mannan and 1,6-α-galactan and through the Fucα1-2Gal, Fucα1-3/4Man, Fucα1-4Xyl, and Fucα1-2Fuc linkages (where Man and Xyl represent D-mannose and D-xylose, respectively), underlying the molecular basis of the FMSinduced IgM antibodies against tumor-specific glycans. mushroom polysaccharide | antitumor activity | anti-Globo H antibody V arious forms of herbal medicine polysaccharides have become valuable as health supplements worldwide (1, 2), suggesting that administration of such polysaccharides may improve innate immunity in vivo. The underlying molecular mechanisms, however, still remain ambiguous. Aberrant terminal fucosylation as well as sialylation in tumor-associated glycans is one of several glycosylation events important in cancer progression (3, 4), and such unusual glycans have recently been used for the development of anticancer vaccines (5-7). As an example, the Globo H-based glycoconjugate vaccines are currently undergoing large-scale clinical trials and have shown promise in therapeutic treatment (8, 9). Studies on the immune response to pathogenic microorganisms (such as Haemophilus influenza type B and Streptococcus pneumonia) have demonstrated that polysaccharides containing repeating antigenic units are generally T cell-independent (TI) (10, 11). Furthermore, recent findings revealed that specific B-cell subsets could establish memory for providing specific Ig synthesis in response to TI-associated polysaccharides (12)(13)(14). In an attempt to understand the biological significance of polysaccharides derived from natural sources, we previously isolated and characterized a crude extract fraction of water-soluble and L-fucose (Fuc)-containing polysaccharides (F3) from Ganoderma lucidum (Reishi) (a mushroom that has been long used as a herb medicine) (15). F3 has since been shown essential for regulation of cytokine network...

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Section: Fuc-enriched F3 Polysaccharide Fraction Induced Antibodies Rsupporting

confidence: 91%

Immunization of fucose-containing polysaccharides from Reishi mushroom induces antibodies to tumor-associated Globo H-series epitopes

Liao

Liang

et al. 2013

Proc. Natl. Acad. Sci. U.S.A.

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“…However, the labeling of the antibody to other H-related and fucosylated structures such as Le y cannot be dismissed. Recently, it has been determined by ELISA with 21 ABH-, Ii-or Lewis-related synthetic oligosaccharides coupled to BSA that, under these conditions, 27 out of 28 anti-H monoclonal antibodies crossreact with related antigens (Mollicone et al 1996). The other antigens that our antibody could recognize could be H type 6 and Le y chains.…”

Section: Localization Of the H Antigenmentioning

confidence: 98%

“…Both oligosaccharides have been demonstrated to be present in the gastrointestinal mucosa (Mollicone et al 1986). H type 6 and Le y were labeled, respectively, by 21 and 10 of the 28 anti-H monoclonal antibodies tested (Mollicone et al 1996).…”

Section: Localization Of the H Antigenmentioning

confidence: 99%

Secretion of fucosylated oligosaccharides related to the H antigen by human gastric cells

Madrid

Leis

Díaz‐Flores

et al. 1998

Histochemistry and Cell Biology

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Although the role of the blood group antigens in the gastrointestinal tract is not well understood, alterations in blood group-related antigens have been described in some pathological processes. Thus, the knowledge of their expression under normal conditions is of special interest. Those individuals expressing their ABO blood group in exocrine epithelia and secretions are called secretors. The aim of the present study was the localization of H antigen expression in the normal human gastric epithelial cells of non-O blood group individuals. For this, a monoclonal anti-H antibody was examined by immunocytochemical methods at both the light and electron microscopic levels. In combination with enzymatic and chemical treatments, the nature of the oligosaccharide chains containing the H antigen was characterized. The selected cases were four A secretors, three A nonsecretors, and three B non-secretors. The labeling of the anti-H antibody in the human stomach is described, irrespective of the blood group of the individuals. The staining was abolished when O-linked oligosaccharides were removed. Since commercially available anti-H antibodies usually also recognize other H-related antigens, the labeling of the antibody by H-related antigens cannot be dismissed. Our findings suggest the existence of H or H-related antigens in the O-linked oligosaccharides of the secretory granules of the surface, gastric pit, mucous neck, and transitional cells of the fundic mucosa, and in the intracellular canaliculi and tubulovesicular system of parietal cells. The H or H-related antigens were also localized in the apical membrane of all the cell types of the epithelial cells of the human fundic mucosa. The overall distribution of the H or H-related antigens in the stomach in non-O blood group individuals suggests the constitutive expression of an alpha(1,2)fucosyltransferase.

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“…After 48 h, H-type 2, Le a and Le x oligosaccharide epitopes were detected on transfected cells by immunofluorescence as described [16]and observed on an epifluorescence microscope [17]. …”

Section: Methodsmentioning

confidence: 99%

Point Mutations and Deletion Responsible for the Bombay H null and the Reunion H weak Blood Groups

Fernández-Mateos¹,

Cailleau²,

Henry³

et al. 1998

Vox Sanguinis

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Objective: Definition of the molecular basis of the Reunion and the Bombay red cell and salivary H-deficient phenotypes. Methods: Sequence and expression of FUT1 and FUT2 genes from H-deficient individuals. Family segregation analysis of the mutations responsible for the fucosyltransferase defects of H, secretor and Lewis systems. Results: The Indian red cell H null Bombay phenotype depends on a new mutation of the FUT1 gene. T725 → G changing Leu242 → Arg. Their salivary nonsecretor phenotype is secondary to a complete deletion of the FUT2 gene. The red cell H weak Reunion phenotype depends on another new mutation of FUT1, C349 → T which induces a change of His117 → Tyr. Their salivary nonsecretor phenotype is due to the known Caucasian inactivating mutation G428 → A. Conclusion: Single prevalent FUT1 and FUT2 point mutations and a deletion are responsible for the Indian Bombay H null and the Reunion H weak phenotypes found on Reunion island. This is in contrast with other H-deficient phenotypes where sporadic nonprevalent inactivating mutations are the rule.

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Recognition of the blood group H type 2 trisaccharide epitope by 28 monoclonal antibodies and three lectins

Cited by 34 publications

References 36 publications

Immunization of fucose-containing polysaccharides from Reishi mushroom induces antibodies to tumor-associated Globo H-series epitopes

Immunization of fucose-containing polysaccharides from Reishi mushroom induces antibodies to tumor-associated Globo H-series epitopes

Secretion of fucosylated oligosaccharides related to the H antigen by human gastric cells

Point Mutations and Deletion Responsible for the Bombay H null and the Reunion H weak Blood Groups

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