Characterization of the binding specificity ofAnguilla anguilla agglutinin (AAA) in comparison toUlex europaeus agglutinin I (UEA-I)

Baldus, Stephan; Thiele, Jüergen; Park, Young-Ok; Hanisch, Franz‐Georg; Bara, Jacques; Fischer, R.

doi:10.1007/bf00731446

Cited by 67 publications

(41 citation statements)

References 24 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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“…75 and 160, respectively). Consistent with early observations of this lectin (Baldus et al, 1996;Debray et al, 1981;Petryniak and Goldstein, 1986;Sughii et al, 1982), the a1-2-linked fucose is an absolute requirement for UEA-I binding. This is based on the observations that the non-fucosylated Galb1-4GlcNAc (LacNAc), which is a component of most of the binding glycans (Supplementary Table S5; see online supplementary material at http:// www.liebertpub.com), is found in over 180 non-binding glycans, lacks fucose addition, and is not bound by UEA-I.…”

Section: Analysis Of Uea-isupporting

confidence: 88%

Automated Motif Discovery from Glycan Array Data

Cholleti

Agravat

Morris

et al. 2012

OMICS: A Journal of Integrative Biology

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Assessing interactions of a glycan-binding protein (GBP) or lectin with glycans on a microarray generates large datasets, making it difficult to identify a glycan structural motif or determinant associated with the highest apparent binding strength of the GBP. We have developed a computational method, termed GlycanMotifMiner, that uses the relative binding of a GBP with glycans within a glycan microarray to automatically reveal the glycan structural motifs recognized by a GBP. We implemented the software with a web-based graphical interface for users to explore and visualize the discovered motifs. The utility of GlycanMotifMiner was determined using five plant lectins, SNA, HPA, PNA, Con A, and UEA-I. Data from the analyses of the lectins at different protein concentrations were processed to rank the glycans based on their relative binding strengths. The motifs, defined as glycan substructures that exist in a large number of the bound glycans and few nonbound glycans, were then discovered by our algorithm and displayed in a web-based graphical user interface (http://glycanmotifminer.emory.edu). The information is used in defining the glycan-binding specificity of GBPs. The results were compared to the known glycan specificities of these lectins generated by manual methods. A more complex analysis was also carried out using glycan microarray data obtained for a recombinant form of human galectin-8. Results for all of these lectins show that GlycanMotifMiner identified the major motifs known in the literature along with some unexpected novel binding motifs.

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“…This indicates that antifungal activity against M. racemosus is a distinctive feature of AAL. The carbohydrate-binding specificity of AAL is substantially different from those of UEA-I and AAA 24) and this specificity might relate to antifungal activity. Alternatively, AAL could have other active sites for antifungal activity, further research is needed to elucidate this.…”

Section: Discussionmentioning

confidence: 95%