Carbohydrate specificity of an insecticidal lectin isolated from the leaves of Glechoma hederacea (ground ivy) towards mammalian glycoconjugates

Preliminary studies indicated that the potent insecticidal lectin, Gleheda, from the leaves of Glechoma hederacea (ground ivy) preferentially agglutinates human erythrocytes carrying the Tn (GalNAcalpha1-Ser/Thr) antigen. However, no details have been reported yet with respect to the fine specificit...

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Published in:Biochemical journal 2006-01, Vol.393 (Pt 1), p.331-341
Main Authors: Singh, Tanuja, Wu, June H, Peumans, Willy J, Rougé, Pierre, Van Damme, Els J M, Alvarez, Richard A, Blixt, Ola, Wu, Albert M
Format: Article
Language:English
Subjects:
Binding Sites
Enzyme-Linked Immunosorbent Assay
Glycoconjugates - chemistry
Glycoconjugates - metabolism
Humans
Insecticides - chemistry
Insecticides - isolation & purification
Insecticides - metabolism
Lamiaceae - chemistry
Lectins - chemistry
Lectins - isolation & purification
Lectins - metabolism
Models, Molecular
Plant Leaves - chemistry
Substrate Specificity
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Summary:Preliminary studies indicated that the potent insecticidal lectin, Gleheda, from the leaves of Glechoma hederacea (ground ivy) preferentially agglutinates human erythrocytes carrying the Tn (GalNAcalpha1-Ser/Thr) antigen. However, no details have been reported yet with respect to the fine specificity of the lectin. To corroborate the molecular basis of the insecticidal activity and physiological function of Gleheda, it is necessary to identify the recognition factors that are involved in the Gleheda-glycotope interaction. In the present study, the requirement of high-density multivalent carbohydrate structural units for Gleheda binding and a fine-affinity profile were evaluated using ELLSA (enzyme-linked lectinosorbent assay) with our extended glycan/ligand collections, a glycan array and molecular modelling. From the results, we concluded that a high-density of exposed multivalent Tn-containing glycoproteins (natural armadillo and asialo ovine salivary glycoproteins) were the most potent factors for Gleheda binding. They were, on a nanogram basis, 6.5x10(5), 1.5x10(4) and 3.1x10(3) times more active than univalent Gal (galactose), GalNAc (N-acetylgalactosamine) and Tn respectively. Among mono- and oligo-saccharides examined, simple clustered Tn (molecular mass
ISSN:0264-6021
1470-8728
DOI:10.1042/BJ20051162