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Plant and Cell Physiology Advance Access originally published online on May 4, 2009
Plant and Cell Physiology 2009 50(6):1142-1155; doi:10.1093/pcp/pcp065
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© The Author 2009. Published by Oxford University Press on behalf of Japanese Society of Plant Physiologists. All rights reserved. For permissions, please email: journals.permissions@oxfordjournals.org

Spodoptera littoralis-Induced Lectin Expression in Tobacco

Gianni Vandenborre1,4, Otto Miersch2, Bettina Hause3, Guy Smagghe4, Claus Wasternack2 and Els J.M. Van Damme1,*

1Laboratory of Biochemistry and Glycobiology, Department of Molecular Biotechnology, Ghent University, Coupure Links 653, B-9000 Ghent, Belgium
2Department of Natural Product Biotechnology, Leibniz Institute of Plant Biochemistry, Weinberg 3, D-06120 Halle (Saale), Germany
3Department of Secondary Metabolism, Leibniz Institute of Plant Biochemistry, Weinberg 3, D-06120 Halle (Saale), Germany
4Laboratory of Agrozoology, Department of Crop Protection, Ghent University, Coupure Links 653, B-9000 Ghent, Belgium

*Corresponding author: E-mail, ElsJM.VanDamme{at}Ugent.be; Fax +32-92646219.


  Abstract

The induced defense response in plants towards herbivores is mainly regulated by jasmonates and leads to the accumulation of so-called jasmonate-induced proteins. Recently, a jasmonate (JA) inducible lectin called Nicotiana tabacum agglutinin or NICTABA was discovered in tobacco (N. tabacum cv Samsun) leaves. Tobacco plants also accumulate the lectin after insect attack by caterpillars. To study the functional role of NICTABA, the accumulation of the JA precursor 12-oxophytodienoic acid (OPDA), JA as well as different JA metabolites were analyzed in tobacco leaves after herbivory by larvae of the cotton leafworm (Spodoptera littoralis) and correlated with NICTABA accumulation. It was shown that OPDA, JA as well as its methyl ester can trigger NICTABA accumulation. However, hydroxylation of JA and its subsequent sulfation and glucosylation results in inactive compounds that have lost the capacity to induce NICTABA gene expression. The expression profile of NICTABA after caterpillar feeding was recorded in local as well as in systemic leaves, and compared to the expression of several genes encoding defense proteins, and genes encoding a tobacco systemin and the allene oxide cyclase, an enzyme in JA biosynthesis. Furthermore, the accumulation of NICTABA was quanti-fied after S. littoralis herbivory and immunofluorescence microscopy was used to study the localization of NICTABA in the tobacco leaf.

Keywords: Agglutinin - Carbohydrate binding - Lectin - Plant insect interaction - Nicotiana tabacum - Nictaba

Abbreviations: BSA, bovine serum albumin; CPI, chymotrypsin proteinase inhibitor; DAB, diaminobenzidine; ELISA, enzyme-linked immunosorbent assay; HRP, horse radish peroxidase; 12-HSO4-JA, 12-hydroxyjasmonic acid sulfate; JA, jasmonic acid; JAZ, jasmonate ZIM-domain protein; JIPs, jasmonate-induced proteins; LOX, lipoxygenase; Me-JA, methyl jasmonate; NICTABA, Nicotiana tabacum agglutinin; 12-O-Glc-JA, 12-hydroxyjasmonic acid glucoside; 11-OH-JA, 11-hydroxyjasmonic acid; 12-OH-JA, 12-hydroxy-jasmonic acid; OPD, O-phenylenediamine hydrochloride; OPDA, 12-oxophytodienoic acid; PBS, phosphate buffered saline; PEG, polyethylene glycol; PI, proteinase inhibitor; PPO, polyphenol oxidase; ppTobHS-A, hydroxyproline-rich glycopeptide systemin precursor A; RT-PCR, reverse transcription-PCR; TPI, trypsin proteinase inhibitor

(Received April 27, 2009; Accepted April 29, 2009)
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