Purification and Characterization of a Lectin from the Beetle, 
            Allomyrina dichotoma

Umetsu, Kazuo; Kosaka, Suezo; Suzuki, Tomohiko

doi:10.1093/oxfordjournals.jbchem.a134590

Cited by 56 publications

(14 citation statements)

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“…The agglutination of cow erythrocytes by the Spli Lec was not affected by heating to 100°C, confirming its thermal stability. This result confirmed the results obtained by Santos et al , [47] who isolated a lectin which was thermostable at 100°C during 7 h. Thermostable lectins were also reported in the coleopteran Allomyrina dichotoma [36], the orthopteran L. migratoria [48] and the culicid C. quinquefasciatus [46]. However, thermal instability is a characteristic of lectins of some other insects, e.g.…”

Section: Discussionsupporting

confidence: 89%

Characterization of Multisugar-Binding C-Type Lectin (SpliLec) from a Bacterial-Challenged Cotton Leafworm, Spodoptera littoralis

2012

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BackgroundVarious proteins that display carbohydrate-binding activity in a Ca2+-dependent manner are classified into the C-type lectin family. They have one or two C-type carbohydrate-recognition domains (CRDs) composed of 110–130 amino acid residues in common. C-type lectins mediate cell adhesion, non-self recognition, and immuno-protection processes in immune responses and thus play significant roles in clearance of invaders, either as cell surface receptors for microbial carbohydrates or as soluble proteins existing in tissue fluids. The lectin of Spodoptera littoralis is still uncharacterized.MethodologyA single orf encoding a deduced polypeptide consisting of an 18-residue signal peptide and a 291-residue mature peptide, termed SpliLec, was isolated from the haemolymph of the cotton leafworm, S. littoralis, after bacterial challenge using RACE-PCR. Sequence analyses of the data revealed that SpliLec consists of two CRDs. Short-form CRD1 and long-form CRD2 are stabilized by two and three highly conserved disulfide bonds, respectively. SpliLec shares homology with some dipteran lectins suggesting possible common ancestor. The purified SpliLec exhibited a 140-kDa molecular mass with a subunit molecular mass of 35 kDa. The hemagglutination assays of the SpliLec confirmed a thermally stable, multisugar-binding C-type lectin that binds different erythrocytes. The purified SpliLec agglutinated microorganisms and exhibited comparable antimicrobial activity against gram (+) and gram (−) bacteria too.ConclusionsOur results suggested an important role of the SpliLec gene in cell adhesion and non-self recognition. It may cooperate with other AMPs in clearance of invaders of Spodoptera littoralis.

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Section: Discussionsupporting

confidence: 89%

Characterization of Multisugar-Binding C-Type Lectin (SpliLec) from a Bacterial-Challenged Cotton Leafworm, Spodoptera littoralis

2012

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“…They included two of galactose binding lectins, peanut agglutinin (PNA) (Lotan et al, 1975) and Allomyrina dichotoma agglutinin (AIIo A) (Umetsu et al, 1984), and two of Nacetylgalactosamine binding lectins, Vic& villosa agglutinin (VVA) (Sherida & Rosalind, 1983) and Wistaria floribunda agglutinin (WFA) (Kurokawa, et al, 1976). They included two of galactose binding lectins, peanut agglutinin (PNA) (Lotan et al, 1975) and Allomyrina dichotoma agglutinin (AIIo A) (Umetsu et al, 1984), and two of Nacetylgalactosamine binding lectins, Vic& villosa agglutinin (VVA) (Sherida & Rosalind, 1983) and Wistaria floribunda agglutinin (WFA) (Kurokawa, et al, 1976).…”

Section: Methodsmentioning

confidence: 99%

A dual staining method for identifying mucins of different gastric epithelial mucous cells

et al. 1991

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A dual staining method has been developed to identify two types of mucous secreting cells in the gastric mucosa of human and rat in one and the same tissue section. Sections were stained first using the galactose oxidase-cold thionin Schiff (GOCTS) procedure and then with paradoxical Concanavalin A staining (PCS). Surface mucous cell mucin stained blue with GOCTS, whereas gland mucous cell mucin stained brown with PCS. This method enabled us to differentiate these two types of mucins not only in gastric epithelial cell cytoplasm but also in the extracellular space. Sugar residues detected by GOCTS were explored by employing four species of lectins, which were peanut and Allomyrina dichotoma agglutinins for beta-galactose and Vicia villosa and Wistaria floribunda agglutinins for beta-N-acetylgalactosamine. The effect of oxidation with galactose oxidase was also examined on the affinities of reactive sites for these lectins. The results indicated that, in the human stomach, the sugar residues responsible for this reactivity were most likely beta-N-acetylgalactosamine and beta-galactose in specimens lacking secretion of blood group determinants and beta-N-acetylgalactosamine in those showing the secretion. In the rat stomach, on the other hand, sugar residues responsible for GOCTS were not elucidated by these lectins.

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“…Sialic acid-binding lectins have been rep o rted to be expressed in m any species o f M an d ib u lata, e.g. A m erican lo bster [47], fresh w ater p raw n [48], black tiger praw n [49] and bee tles [50], and in m any species o f M ollusca, e.g. snails [5 1 -5 4 ], sea slug [55], sea m ussel [56] and pacific oyster [57].…”

Section: Invertebratesmentioning

confidence: 99%

Sialic Acid-Binding Proteins: Characterization, Biological Function and Application

Zeng

Gabius

1992

Zeitschrift Für Naturforschung C

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The last decade has witnessed steadily growing support for the notion that the carbohydrate portion of glycoconjugates is not merely an inert structural addition to the protein or lipid backbone. Considerable attention has been given to the chemical composition o f glycosidic residues in such heteropolymers. Sialic acids are frequently occurring components o f oligosac charide side chains in glycoconjugates of most higher animals and a few microorganisms. They appear to play an important role as ligands in glycobiological interactions. Mediation of a proposed protein-carbohydrate recognition will necessarily involve a binding protein with the respective specificity. Such proteins thus are able to serve as receptors for certain types of carbohydrate moieties like sialic acids in vivo. Various members of this class o f proteins have already proven their value as analytical tools in studying expression and localization o f de fined sialoglycoconjugates. These proteins attract much attention due to both their functions in situ and their potential as laboratory tools in glycoconjugate research in areas like biochem istry or histology. We present a survey of the purification, characterization and application of this class o f proteins to illustrate the status of knowledge and the current directions of research in this field.In v ite d T re n d s A rticle

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Purification and Characterization of a Lectin from the Beetle, Allomyrina dichotoma

Cited by 56 publications

References 0 publications

Characterization of Multisugar-Binding C-Type Lectin (SpliLec) from a Bacterial-Challenged Cotton Leafworm, Spodoptera littoralis

Characterization of Multisugar-Binding C-Type Lectin (SpliLec) from a Bacterial-Challenged Cotton Leafworm, Spodoptera littoralis

A dual staining method for identifying mucins of different gastric epithelial mucous cells

Sialic Acid-Binding Proteins: Characterization, Biological Function and Application

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