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Published on October 17, 2002; 10.1104/pp.006684

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Received April 5, 2002
Returned for revision May 13, 2002
Accepted July 3, 2002

Role of the Arginyl-Glycyl-Aspartic Motif in the Action of Ptr ToxA Produced by Pyrenophora tritici-repentis

Steven W. Meinhardt *, Weijun Cheng , Chil Y. Kwon , Christine M. Donohue , and Jack B. Rasmussen

Department of Biochemistry (S.W.M., W.C.) and Department of Plant Pathology (C.Y.K., C.M.D., J.B.R.), North Dakota State University, Fargo, North Dakota 58105

* Corresponding author; email: steven.meinhardt{at}ndsu.nodak.edu.

A fundamental problem of plant science is to understand the biochemical basis of plant/pathogen interactions. The foliar disease tan spot of wheat (Triticum aestivum), caused by Pyrenophora tritici-repentis, involves Ptr ToxA, a proteinaceous host-selective toxin that causes host cell death. The fungal gene ToxA encodes a 17.2-kD pre-pro-protein that is processed to produce the mature 13.2-kD toxin. Amino acids 140 to 142 of the pre-pro-protein form an arginyl-glycyl-aspartic (RGD) sequence, a motif involved in the binding of some animal proteins and pathogens to transmembrane receptor proteins called integrins. Integrin-like proteins have been identified in plants recently, but their role in plant biology is unclear. Our model for Ptr ToxA action predicts that toxin interacts with a putative host receptor through the RGD motif. Mutant clones of a ToxA cDNA, created by polymerase chain reaction such that the RGD in the pro-toxin was changed to arginyl-alanyl-aspartic or to arginyl-glycyl-glutamic, were expressed in Escherichia coli. Extracts containing mutated forms of toxin failed to cause host cell death, but extracts from E. coli expressing both a wild-type pro-protein cDNA and a control mutation away from RGD were active in cell death development. In competition experiments, 2 mM RGD tripeptide reduced the level of electrolyte leakage from wheat leaves by 63% when co-infiltrated with purified Ptr ToxA (15 µg mL-1) obtained from the fungus, but the control peptide arginyl-glycyl-glutamyl-serine provided no protection. These experiments indicate that the RGD motif of Ptr ToxA is involved with toxin action, possibly by interacting with a putative integrin-like receptor in the host.




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