Plant Physiology Preview
Published on October 3, 2002; 10.1104/pp.007427
Received April 23, 2002
Returned for revision June 10, 2002
Accepted June 23, 2002
Mass Spectrometric Identification of Isoforms of PR Proteins in Xylem Sap of Fungus-Infected Tomato
Martijn Rep *, Henk L. Dekker , Jack H. Vossen , Albert D. de Boer , Petra M. Houterman , Dave Speijer , Jaap W. Back , Chris G. de Koster , and Ben J.C. Cornelissen
Plant Pathology, Swammerdam Institute for Life Sciences, University of Amsterdam, P.O. Box 94062, 1090 GB Amsterdam, The Netherlands (M.R., J.H.V., A.D.d.B., P.M.H., B.J.C.C.); Mass Spectrometry, Swammerdam Institute for Life Sciences, University of Amsterdam, Nieuwe Achtergracht 166, 1018 WV Amsterdam, The Netherlands (H.L.D., J.W.B., C.G.d.K.); and Biochemistry, Academic Medical Center, Meibergdreef 15, 1105 AZ, Amsterdam, The Netherlands (D.S.)
* Corresponding author; email: rep{at}science.uva.nl.
The protein content of tomato (Lycopersicon esculentum) xylem sap was found to change dramatically upon infection with the vascular wilt fungus Fusarium oxysporum. Peptide mass fingerprinting and mass spectrometric sequencing were used to identify the most abundant proteins appearing during compatible or incompatible interactions. A new member of the PR-5 family was identified that accumulated early in both types of interaction. Other pathogenesis-related proteins appeared in compatible interactions only, concomitantly with disease development. This study demonstrates the feasibility of using proteomics for the identification of known and novel proteins in xylem sap, and provides insights into plant-pathogen interactions in vascular wilt diseases.
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