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.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Sequence
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Base Sequence
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DNA, Complementary
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Fusarium / growth & development*
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Glucan 1,3-beta-Glucosidase*
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Glycoside Hydrolases / isolation & purification
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Glycoside Hydrolases / metabolism
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Immunity, Innate
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Mass Spectrometry / methods*
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Molecular Sequence Data
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Phylogeny
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Plant Diseases / genetics
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Plant Diseases / microbiology*
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Plant Proteins / chemistry
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Plant Proteins / genetics
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Plant Proteins / metabolism*
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Plant Structures / genetics
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Plant Structures / metabolism*
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Plant Structures / microbiology
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Protein Isoforms / chemistry
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Protein Isoforms / genetics
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Protein Isoforms / metabolism
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Proteomics / methods
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Sequence Homology, Amino Acid
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Sequence Homology, Nucleic Acid
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Solanum lycopersicum / genetics
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Solanum lycopersicum / metabolism*
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Solanum lycopersicum / microbiology
Substances
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DNA, Complementary
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Plant Proteins
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Protein Isoforms
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pathogenesis-related proteins, plant
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Glycoside Hydrolases
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Glucan 1,3-beta-Glucosidase
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beta-1,3-exoglucanase