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      Mass spectrometric identification of isoforms of PR proteins in xylem sap of fungus-infected tomato.

      Plant physiology
      Amino Acid Sequence, Base Sequence, DNA, Complementary, Fusarium, growth & development, Glucan 1,3-beta-Glucosidase, Glycoside Hydrolases, isolation & purification, metabolism, Immunity, Innate, Lycopersicon esculentum, genetics, microbiology, Mass Spectrometry, methods, Molecular Sequence Data, Phylogeny, Plant Diseases, Plant Proteins, chemistry, Plant Structures, Protein Isoforms, Proteomics, Sequence Homology, Amino Acid, Sequence Homology, Nucleic Acid

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          Abstract

          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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