Mass Spectrometric Identification of Isoforms of PR Proteins in Xylem Sap of Fungus-Infected Tomato
Author(s) -
Martijn Rep,
Henk L. Dekker,
Jack H. Vossen,
Albert D. de Boer,
Petra M. Houterman,
Dave Speijer,
Jaap Willem Back,
Chris G. de Koster,
Ben J. C. Cornelissen
Publication year - 2002
Publication title -
plant physiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.554
H-Index - 312
eISSN - 1532-2548
pISSN - 0032-0889
DOI - 10.1104/pp.007427
Subject(s) - xylem , wilt disease , biology , fungus , fusarium oxysporum , proteomics , lycopersicon , botany , identification (biology) , gene isoform , pathogen , peptide mass fingerprinting , microbiology and biotechnology , biochemistry , gene
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.
Accelerating Research
Robert Robinson Avenue,
Oxford Science Park, Oxford
OX4 4GP, United Kingdom
Address
John Eccles HouseRobert Robinson Avenue,
Oxford Science Park, Oxford
OX4 4GP, United Kingdom