4.5 Article

Molecular Dissection of Extracellular Matrix Proteome Reveals Discrete Mechanism Regulating Verticillium Dahliae Triggered Vascular Wilt Disease in Potato

Journal

PROTEOMICS
Volume 17, Issue 23-24, Pages -

Publisher

WILEY
DOI: 10.1002/pmic.201600373

Keywords

comparative proteomics; extracellular matrix; patho-stress; potato; vascular wilt; Verticillium dahliae

Funding

  1. National Institute of Plant Genome Research, New Delhi, India
  2. Department of Biotechnology, Govt. of India [BT/HRD/35/01/05/2013]
  3. DBT-TWAS
  4. Department of Biotechnology (DBT), Govt. of India
  5. Council of Scientific and Industrial research (CSIR), Govt. of India

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Plants exposed to patho-stress mostly succumb due to disease by disruption of cellular integrity and changes in the composition of the extracellular matrix (ECM). Vascular wilt, caused by the soil borne hemibiotrophic filamentous fungus Verticillium dahliae, is one of the most significant diseases that adversely affect plant growth and productivity. The virulence of the pathogen associated with the ECM-related susceptibility of the host plant is far from being understood. To better understand ECM-associated disease responses that allow the pathogen to suppress plant immunity, a temporal analysis of ECM proteome was carried out in vascular wilt susceptible potato cultivar upon V. dahliae infection. The proteome profiling led to the identification of 75 patho-stress responsive proteins (PSRPs), predominantly involved in wall hydration, architecture, and redox homeostasis. Two novel clues regarding wilt disease of potato were gained from this study. First, wall crosslinking and salicylic acid signaling significantly altered during patho-stress. Second, generation of reactive oxygen species and scavenging proteins increased in abundance leading to cell death and necrosis of the host. We provide evidence for the first time that how fungal invasion affects the integrity of ECM components and host reprogramming for susceptibility may function at the cell surface by protein plasticity.

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