Pathogen elicitor-induced changes in the maize extracellular matrix proteome

Chivasa, S; Simon, WJ; Yu, XL; Yalpani, N; Slabas, AR

Abstract

The extracellular matrix is a vital compartment in plants with a prominent role in defence against pathogen attack. Using a maize cell suspension culture system and pathogen elicitors, responses to pathogen attack that are localised to the extracellular matrix were examined by a proteomic approach. Elicitor treatment of cell cultures induced a rapid change in the phosphorylation status of extracellular peroxidases, the apparent disappearance of a putative extracellular beta-N-acetylglucosamonidase, and accumulation of a secreted putative xylanase inhibitor protein. Onset of the defence response was attended by an accumulation of glyceraldehyde-3-phosphate dehydrogenase and a fragment of a putative heat shock protein. Several distinct spots of both proteins, which preferentially accumulated in cell wall protein fractions, were identified. These three novel observations, viz. (i) secretion of a new class of putative enzyme inhibitor, (ii) the apparent recruitment of classical cytosolic proteins into the cell wall and (ii) the change in phosphorylation status of extracellular matrix proteins, suggest that the extracellular matrix plays a complex role in defence. We discuss the role of the extracellular matrix in signal modulation during pathogen-induced defence responses.

Citation

Chivasa, S., Simon, W., Yu, X., Yalpani, N., & Slabas, A. (2005). Pathogen elicitor-induced changes in the maize extracellular matrix proteome. Proteomics, 5(18), 4894-4904. https://doi.org/10.1002/pmic.200500047

• Journal Article Type: Article
• Publication Date: Dec 1, 2005
• Deposit Date: Jan 18, 2008
• Journal: Proteomics
• Print ISSN: 1615-9853
• Electronic ISSN: 1615-9861
• Publisher: Wiley
• Peer Reviewed: Peer Reviewed
• Volume: 5
• Issue: 18
• Pages: 4894-4904
• DOI: https://doi.org/10.1002/pmic.200500047
• Keywords: Dehydrogenase, Extracellular matrix, Glyceraldehyde-3-phosphate, Heat shock protein-82, Maize, Phosphotyrosine.
• Public URL: https://durham-repository.worktribe.com/output/1557986