Sialic acid-specific lectins: occurrence, specificity and function

Lehmann, Friederike; Tiralongo, Evelin; Tiralongo, Joe

doi:10.1007/s00018-005-5589-y

Cited by 209 publications

(210 citation statements)

References 272 publications

(92 reference statements)

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“…Sialylation occurs mostly in mammals, birds, and their pathogenic microorganisms, in which it acts in recognition phenomena (Vimr and Lichtensteiger, 2002;Schauer, 2009). The recognition of 9NAcNeu 5 Ac by PP2-A1 may thus facilitate binding to sialylated proteins from animal herbivores, as suggested for other plant lectins from this group (Lehmann et al, 2006). PP2-A1-His 6 also bound high-Man N-linked glycans, with a common Man 3 GlcNAc 2 core structure, which was recognized with high affinity (Fig.…”

Section: Pp2-a1 Binds To Different Classes Of Glycansmentioning

confidence: 64%

“…PP2-A1-His 6 bound 9NAcNeu 5 Ac with high affinity. Sialic acids are present neither in plants nor in their pathogens, although a few sialic acid-specific plant lectins are known (Lehmann et al, 2006;Zeleny et al, 2006). Sialylation occurs mostly in mammals, birds, and their pathogenic microorganisms, in which it acts in recognition phenomena (Vimr and Lichtensteiger, 2002;Schauer, 2009).…”

Section: Pp2-a1 Binds To Different Classes Of Glycansmentioning

confidence: 99%

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Binding Properties of the N-Acetylglucosamine and High-Mannose N-Glycan PP2-A1 Phloem Lectin in Arabidopsis

et al. 2010

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Phloem Protein2 (PP2) is a component of the phloem protein bodies found in sieve elements. We describe here the lectin properties of the Arabidopsis (Arabidopsis thaliana) PP2-A1. Using a recombinant protein produced in Escherichia coli, we demonstrated binding to N-acetylglucosamine oligomers. Glycan array screening showed that PP2-A1 also bound to highmannose N-glycans and 9-acyl-N-acetylneuraminic sialic acid. Fluorescence spectroscopy-based titration experiments revealed that PP2-A1 had two classes of binding site for N,N#,N$-triacetylchitotriose, a low-affinity site and a high-affinity site, promoting the formation of protein dimers. A search for structural similarities revealed that PP2-A1 aligned with the Cbm4 and Cbm22-2 carbohydrate-binding modules, leading to the prediction of a b-strand structure for its conserved domain. We investigated whether PP2-A1 interacted with phloem sap glycoproteins by first characterizing abundant Arabidopsis phloem sap proteins by liquid chromatography-tandem mass spectrometry. Then we demonstrated that PP2-A1 bound to several phloem sap proteins and that this binding was not completely abolished by glycosidase treatment. As many plant lectins have insecticidal activity, we also assessed the effect of PP2-A1 on weight gain and survival in aphids. Unlike other mannosebinding lectins, when added to an artificial diet, recombinant PP2-A1 had no insecticidal properties against Acyrthosiphon pisum and Myzus persicae. However, at mid-range concentrations, the protein affected weight gain in insect nymphs. These results indicate the presence in PP2-A1 of several carbohydrate-binding sites, with potentially different functions in the trafficking of endogenous proteins or in interactions with phloem-feeding insects.

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Section: Pp2-a1 Binds To Different Classes Of Glycansmentioning

confidence: 64%

Section: Pp2-a1 Binds To Different Classes Of Glycansmentioning

confidence: 99%

Binding Properties of the N-Acetylglucosamine and High-Mannose N-Glycan PP2-A1 Phloem Lectin in Arabidopsis

et al. 2010

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“…H ost surface glycosylation is ubiquitous and is targeted by pathogenic bacteria, viruses, fungi and parasites for adherence and toxin binding and by glycosidases (1). Escherichia coli type 1 fimbriae, FimH, is one of the most widely studied glycanrecognizing protein adhesins, with specificity for monomannose to oligomannose structures with the variability of the mannose structure bound leading to different tissue tropism (2).…”

mentioning

confidence: 99%

Glycan:glycan interactions: High affinity biomolecular interactions that can mediate binding of pathogenic bacteria to host cells

Day

Tran

Semchenko

et al. 2015

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

107

104

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Cells from all domains of life express glycan structures attached to lipids and proteins on their surface, called glycoconjugates. Cell-tocell contact mediated by glycan:glycan interactions have been considered to be low-affinity interactions that precede highaffinity protein-glycan or protein-protein interactions. In several pathogenic bacteria, truncation of surface glycans, lipooligosaccharide (LOS), or lipopolysaccharide (LPS) have been reported to significantly reduce bacterial adherence to host cells. Here, we show that the saccharide component of LOS/LPS have direct, high-affinity interactions with host glycans. Glycan microarrays reveal that LOS/LPS of four distinct bacterial pathogens bind to numerous host glycan structures. Surface plasmon resonance was used to determine the affinity of these interactions and revealed 66 high-affinity host-glycan:bacterial-glycan pairs with equilibrium dissociation constants (K D ) ranging between 100 nM and 50 μM. These glycan:glycan affinity values are similar to those reported for lectins or antibodies with glycans. Cell assays demonstrated that glycan:glycan interaction-mediated bacterial adherence could be competitively inhibited by either host cell or bacterial glycans. This is the first report to our knowledge of high affinity glycan:glycan interactions between bacterial pathogens and the host. The discovery of large numbers of glycan:glycan interactions between a diverse range of structures suggests that these interactions may be important in all biological systems.H ost surface glycosylation is ubiquitous and is targeted by pathogenic bacteria, viruses, fungi and parasites for adherence and toxin binding and by glycosidases (1). Escherichia coli type 1 fimbriae, FimH, is one of the most widely studied glycanrecognizing protein adhesins, with specificity for monomannose to oligomannose structures with the variability of the mannose structure bound leading to different tissue tropism (2). Other glycan-recognizing adhesins expressed by bacteria include the following: Pseudomonas aeruginosa lectins 1 and 2 (PA-IL and PA-IIL) that have specificity for galactose and fucose, respectively (3); Helicobacter pylori SabA, specific for sialic acid containing glycoconjugates including sialyLewis X; and BabAspecific for fucosylated glycoconjugates including Lewis B (4, 5). Although there are numerous known glycan binding adhesins, the adhesins of some bacteria that interact with host surface glycans remain unknown.Direct interactions between surface glycans (glycan:glycan interactions) have been reported in sea sponges as heterogenous glycan interactions, and in mouse embryo development and cancer where homodimers of Lewis X (LeX) or ganglioside structures play a role in cell adhesion and growth factor receptor interactions (6, 7). Outside of these reports, glycan:glycan interactions, when noted, have generally been considered to be low-affinity, weak interactions (8) that precede high-affinity protein:glycan or protein:protein interactions (1, 2, 5, 9).Interestingly, there...

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“…Epidemiology and histopaphology are among the most studied aspects of schistosomiasis since then (Rutitzky et al, 2005). Molecular, immunohistochemical and histochemical techniques are used to investigate the development of Schistosoma eggs and the role of their secretions in the initiation, development and activation of immune response in the host tissues (Ashton et al, 2001;Lehmann et al).…”

Section: Discussionmentioning

confidence: 99%

“…Lectins, carbohydrate-binding ubiquitous proteins, have found numerous applications in biological and medical areas due to their broad recognition properties (Lehmann et al, 2006). They have been used as probes for prognosis and/or diagnosis in human and animal diseases (Mitchell & Schumacher, 1999).…”

Section: Introductionmentioning

confidence: 99%

Carbohydrates Detection in the Hepatic Egg - Granuloma System Using Lectin Histochemistry

et al. 2008

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MELO-JÚNIOR, M. R.; CAVALCANTI, C. L. B.; DE PONTES-FILHO, N. T.; DE CARVALHO JR, L. B. & BELTRÃO, E. I. C.Carbohydrates detection in the hepatic egg-granuloma system using lectin histochemistry. Int. J. Morphol.,26(4):967-972, 2008. SUMMARY:This study aims to evaluate the egg-granuloma system in hepatic tissues using lectin histochemistry in experimental Schistosomiasis. Eight Swiss mice were infected with a local strain of Schistosoma mansoni, being submitted forty days later to a perfusion after which slices of liver (4µ m) were prepared. The tissue samples were incubated with the following peroxidase conjugated lectins: Peanut agglutinin (PNA), Wheat Germ agglutinin (WGA), and Concanavalin A (Con A). All lectins recognized the glycoconjugates in the adult worm tegument. In the hepatic tissue, WGA presented the highest staining followed by PNA and Con A. The PNA presented the most intense staining of the egg-granuloma system while WGA stained the hepatic sinusoid cells and Con A bound preferentially the fibrosis rings of granuloma and the surrounding hepatic parenquima. WGA and PNA indicated the presence of residues of N-acetyl-glucosamine and galactose in the surface of Schistosoma mansoni eggs in the hepatic granulomas. In conclusion, using PNA, Con A and WGA our study presented different aspects of the egg-granuloma and Tegument of Schistosoma mansoni as well as indicated differences in the peri-ovular granulomas indicating alterations in the cellular mechanism of expression of surface carbohydrates during progression of the Schistosomiasis.

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Sialic acid-specific lectins: occurrence, specificity and function

Cited by 209 publications

References 272 publications

Binding Properties of the N-Acetylglucosamine and High-Mannose N-Glycan PP2-A1 Phloem Lectin in Arabidopsis

Binding Properties of the N-Acetylglucosamine and High-Mannose N-Glycan PP2-A1 Phloem Lectin in Arabidopsis

Glycan:glycan interactions: High affinity biomolecular interactions that can mediate binding of pathogenic bacteria to host cells

Carbohydrates Detection in the Hepatic Egg - Granuloma System Using Lectin Histochemistry

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