Primary structure of an N-glycosidic carbohydrate unit derived from Sophora japonica lectin

Fournet, Bernard; Leroy, Y.; Wieruszeski, Jean‐Michel; Montreuil, Jean; Poretz, R. D.; Goldberg, R.

doi:10.1111/j.1432-1033.1987.tb13517.x

Cited by 67 publications

(18 citation statements)

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“…9 a) is seen for the lectin from Sophora japonica, a member of a different tribe of the Legwninoseae. That these similarities in oligosaccharide 'fingerprints' are indicators of structural similarity is seen in both the present report and that of Fournet et al [45]. We and these authors, independently, isolated glycopeptides from the lectins of E. corallodendron and S. japonica, respectively.…”

Section: Discussionsupporting

confidence: 53%

The beta1 2-d-xylose and alpha1 3-l-fucose substituted N-linked oligosaccharides from Erythrina cristagalli lectin. Isolation, characterisation and comparison with other legume lectins

et al. 1987

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The carbohydrate moieties of Erythrina cristagalli lectin were released as oligosaccharides by hydrazinolysis, followed by N-acetylation and reduction with NaB3H4. Fractionation of the tritium-labelled oligosaccharide mixture by Bio-Gel P-4 column chromatography and high-voltage borate electrophoresis revealed that it is composed of five neutral oligosaccharides. Structural studies by sequential exoglycosidase digestion in combination with methylation analysis and two-dimensional 'H-NMR showed that the major component was the fucosecontaining heptasaccharide Mancr3(Mancr6)(Xylfl2)Manfl4GlcNAcfl4(Fucc3)GlcNAcol. This is the first report of such a structure in plant lectins. Small amounts of the corresponding afucosyl hexasaccharide were also identified, as well as three other minor components.The structure of the heptasaccharide shows the twin characteristics of a newly established family of N-linked glycans, found to date only in plants. The characteristics are substitution of the common pentasaccharide core [Mana3(Mana6)Manfl4GlcNAcfl4GlcNAc] by (1) a D-xylose residue linked 61 -2 to the P-mannosyl residue and (2) an L-fucose residue linked a 1 4 3 to the reducing terminal N-acetylglucosamine residue.The oligosaccharide heterogeneity pattern for Erythrina cristagalli lectin was also found for the lectins from four other Erythrina species and the lectins of two other legumes, Sophora japonica and Lonchocarpus capassa.All species of the genus Erythrina tested contain Nacetyllactosamine-specific lectins that are remarkably similar in their properties [l, 21. These molecules are all glycoproteins (3 -10% neutral carbohydrate by weight) with M , approximately 60000 and are composed of two identical or nearly identical subunits. Their amino acid composition is very similar and a high degree of homology exists in the N-terminal sequences. [20] and more recently for sycamore cell culture laccase [21] and Caesalpinia pulcherrimu protease inhibitor [22].The simultaneous presence of xylose and fucose therefore appears to be a common feature of many plant glycoproteins. This combination has only been described in glycoproteins of animal origin for Helix pomatiu a-haemocyanin [23].In this paper we describe the isolation of the asparaginelinked oligosaccharides of E. cristagalli lectin, their separation by high-resolution gel permeation chromatography and highvoltage electrophoresis and their characterisation by a combination of methylation analysis, nuclear magnetic resonance and sequential exoglycosidase digestion. We also compare the oligosaccharides of E. cristagalli lectin with those of the lectins from four other species of Erythrina (E. corallodendron, E. caffra, E. latissima and E. lysistemon) and the unrelated legumes Lonchocarpus capassa and Sophora japonica.

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Section: Discussionsupporting

confidence: 53%

The beta1 2-d-xylose and alpha1 3-l-fucose substituted N-linked oligosaccharides from Erythrina cristagalli lectin. Isolation, characterisation and comparison with other legume lectins

et al. 1987

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“…Second, the structure (of the minor form) is extended with an additional GlcNAc rather than a mannose. On the other hand, the major carbohydrate moiety of GP-II appears to be identical to those found in several species: a lectin isolated from the seeds of the Japanese pagoda tree (Sophora japonica) [28], laccase a from sycamore cells (Acer pseudoplatanus) [29] and the S-glycoprotein of Brassica campestris [30]. Although we have not yet established which of the terminal mannose residues the additional GlcNAc residue is attached to in GP-II, both possible forms have been found in Acer pseudoplatanus (laccase b1 and b2) and one in S-protein isolated from Brassica compestris [13].…”

Section: Discussionmentioning

confidence: 99%

Amino‐acid sequence and glycan structures of cysteine proteases with proline specificity from ginger rhizome Zingiber officinale

Choi

Laursen

2000

European Journal of Biochemistry

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The ginger proteases (GP-I and GP-II), isolated from the ginger rhizome Zingiber officinale, have an unusual substrate specificity preference for cleaving peptides with a proline residue at the P 2 position. The complete amino-acid sequence of GP-II, a glycoprotein containing 221 amino acids, and about 98% that of GP-I have been determined. Both proteases, which are 82% similar, have cysteine residues at positions 27 and histidines at position 161, corresponding to the essential cysteine±histidine diads found in the papain family of cysteine proteases, and six corresponding cysteine residues that form the three invariant disulfide linkages seen in this family of proteins. The sequence homology with other members (papain, bromelain, actinidin, protease omega, etc.) of this family is < 50%. GP-II has two predicted glycosylation sites at Asn99 and Asn156. Analyisis by electrospray and collision-induced dissociation MS showed that both sites were occupied by the glycans (Man) 3 (Xyl) 1 (Fuc) 1 (GlcNAc) 2 and (Man) 3 (Xyl) 1 (Fuc) 1 (GlcNAc) 3 , in a ratio of < 7 : 1. Both glycans are xylose containing biantennary complex types that share the common core structural unit, Man136(Man133) (Xyl132)Man134GlcNAc134(Fuc133)GlcNAc for the major form, with an additional N-acetylglucosamine residue being linked, in the minor form, to one of the terminal mannose units of the core structure.Keywords: amino-acid sequence; cysteine protease; ginger; glycoprotein; glycosylation site; proline peptidase; proteinase; mass spectrometry. Some 20 families of peptidases dependent on a cysteine residue at the active center are known [1]. The most prominent of these is the papain family, which includes peptidases with a wide variety of activities, including endopeptidases with broad specificity (e.g. papain) and narrow specificity (glycyl endopeptidase), amino peptidases, and a dipeptidyl peptidase. Enzymes of the papain family are found in a wide variety of life forms: baculovirus, eubacteria, yeast, probably all protozoa, plants and animals. Papain homologs are generally either lysosomal (vacuolar) or secreted proteins. In plants, they are found in the vacuoles, but also extracellularly, as in the latex of papaya or fig. Plant cysteine proteinases include papain from papaya (Carica papaya), bromelain from pineapple stem and actinidin from the Chinese gooseberry or kiwi fruit (Actinidia chinensis) [1].Ginger proteases from ginger rhizome, Zingiber officinale, were first reported by Ichikawa et al.[2] in 1973. Two proteases, designated GP-I and GP-II were isolated by chromatography on DEAE-cellulose and tentatively classified as cysteine proteases based on their inhibition by thiol reagents and their relative molecular masses, estimated at < 22 500 by gel filtration. More recently, these proteases were separated as mercuribenzoate derivatives into three fractions by IEF [3]. It has been reported [4] that these proteases have both proteinase and collagenase activities; ginger root extracts have also been tested as a meat tenderizer [5,6].Rec...

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“…The xylose residue is recognized by a set of structural reporter-group signals, namely H-I, H-2, H-3 and H5a at 6 4.463, 6 3.373, 6 3.449 and 6 3.257, respectively (Van Kuik et al, 1985;Fournet et al, 1987).…”

Section: Isolation Of Glycopeptidesmentioning

confidence: 99%

¹H‐NMR structural determination of the N‐linked carbohydrate chains on glycopeptides obtained from the bean lectin phytohemagglutinin

Sturm¹,

Bergwerff²,

Vliegenthart³

1992

European Journal of Biochemistry

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Phytohemagglutinin, the lectin of the common bean Phaseolus vulgaris, is a N-linked glycoprotein with one high-mannose-type and one xylose-containing oligosaccharide side chain per polypeptide. The high-mannose-type glycan is attached to Asnl2 and the complex-type glycan to Am60 [Sturm, A. & Chrispeels, M. J. (1986) Plant Physiol. 81, 320-3221. The structures of the oligosaccharides were elucidated from two glycopeptides obtained from the lectin by Pronase digestion, affinity chromatography on concanavalin-A -Sepharose and gel-filtration chromatography on a column of BioGel P-4. The N-linked glycan structures were investigated by 500-MHz 'H-NMR spectroscopy and were established to be:M m a ( l-Z)Mana( 1-6) D3

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Primary structure of an N-glycosidic carbohydrate unit derived from Sophora japonica lectin

Cited by 67 publications

References 14 publications

The beta1 2-d-xylose and alpha1 3-l-fucose substituted N-linked oligosaccharides from Erythrina cristagalli lectin. Isolation, characterisation and comparison with other legume lectins

The beta1 2-d-xylose and alpha1 3-l-fucose substituted N-linked oligosaccharides from Erythrina cristagalli lectin. Isolation, characterisation and comparison with other legume lectins

Amino‐acid sequence and glycan structures of cysteine proteases with proline specificity from ginger rhizome Zingiber officinale

¹H‐NMR structural determination of the N‐linked carbohydrate chains on glycopeptides obtained from the bean lectin phytohemagglutinin

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Primary structure of an N-glycosidic carbohydrate unit derived from Sophora japonica lectin

Cited by 67 publications

References 14 publications

The beta1 2-d-xylose and alpha1 3-l-fucose substituted N-linked oligosaccharides from Erythrina cristagalli lectin. Isolation, characterisation and comparison with other legume lectins

The beta1 2-d-xylose and alpha1 3-l-fucose substituted N-linked oligosaccharides from Erythrina cristagalli lectin. Isolation, characterisation and comparison with other legume lectins

Amino‐acid sequence and glycan structures of cysteine proteases with proline specificity from ginger rhizome Zingiber officinale

1H‐NMR structural determination of the N‐linked carbohydrate chains on glycopeptides obtained from the bean lectin phytohemagglutinin

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¹H‐NMR structural determination of the N‐linked carbohydrate chains on glycopeptides obtained from the bean lectin phytohemagglutinin