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Published on June 12, 2003; 10.1104/pp.103.023853

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Received March 19, 2003
Returned for revision March 26, 2003
Accepted March 30, 2003

The Tn Antigen-Specific Lectin from Ground Ivy Is an Insecticidal Protein with an Unusual Physiology

Weifang Wang , Bettina Hause , Willy J. Peumans , Guy Smagghe , Anne Mackie , Robin Fraser , and Els J.M. Van Damme *

Department of Molecular Biotechnology (W.W., E.J.M.V.D.), and Laboratory of Agrozoology, Department of Crop Protection (G.S.), Ghent University, Coupure Links 653, 9000 Gent, Belgium; Institute of Plant Biochemistry, P.O.B. 110432, D-06018 Halle, Germany (B.H.); Laboratory for Phytopathology and Plant Protection, Katholieke Universiteit Leuven, Willem de Croylaan 42, 3001 Leuven, Belgium (W.J.P.); West of Scotland Blood Transfusion Centre, Gartnavel General Hospital, 25 Shelley Road, G12 0XB Glasgow, United Kingdom (A.M., R.F.)

* Corresponding author; email: ElsJM.VanDamme{at}rug.ac.be.

Leaves of ground ivy (Glechoma hederacea) contain a lectin (called Gleheda) that is structurally and evolutionary related to the classical legume lectins. Screening of a population of wild plants revealed that Gleheda accounts for more than one-third of the total leaf protein in some clones, whereas it cannot be detected in other clones growing in the same environment. Gleheda is predominantly expressed in the leaves where it accumulates during early leaf maturation. The lectin is not uniformly distributed over the leaves but exhibits a unique localization pattern characterized by an almost exclusive confinement to a single layer of palisade parenchyma cells. Insect feeding trials demonstrated that Gleheda is a potent insecticidal protein for larvae of the Colorado potato beetle (Leptinotarsa decemlineata). Because Gleheda is not cytotoxic, it is suggested that the insecticidal activity is linked to the carbohydrate-binding specificity of the lectin, which as could be demonstrated by agglutination assays with different types of polyagglutinable human erythrocytes is specifically directed against the Tn antigen structure (N-acetylgalactosamine O-linked to serine or threonine residues of proteins).




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