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BIOCHEMICAL PROCESSES AND MACROMOLECULAR STRUCTURES

The Tn Antigen-Specific Lectin from Ground Ivy Is an Insecticidal Protein with an Unusual Physiology¹

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.)

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).

¹ This work was supported in part by the Fund for Scientific Research-Flanders (Belgium; grant no. G.0113.01). W.W. received scholarships from the Education Ministry of China, the Flemish Community, the Catholic University of Leuven, and Ghent University to finish her PhD research.

^* Corresponding author; e-mail ElsJM.VanDamme{at}rug.ac.be; fax 32–9–264–6219.

Received March 19, 2003; returned for revision March 26, 2003; accepted March 30, 2003.

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