First published online October 3, 2002; 10.1104/pp.007427
Plant Physiol, October 2002, Vol. 130, pp. 904-917
Mass Spectrometric Identification of Isoforms of PR Proteins in
Xylem Sap of Fungus-Infected Tomato1
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.)
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.
1
This work was supported in part by the Council
for Medical Sciences of the Netherlands Organization for Scientific Research.
*
Corresponding author; e-mail rep{at}science.uva.nl; fax
31-20-5257934.
© 2002 American Society of Plant Physiologists
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