HOMEPRODUCTSCOMPANYCONTACTFAQResearchDictionaryPharmaSign Up FREE or Login

The apoplastic oxidative burst in response to biotic stress in plants: a three-component system.

Abstract
The oxidative burst, the generation of reactive oxygen species (ROS) in response to microbial pathogen attack, is a ubiquitous early part of the resistance mechanisms of plant cells. It has also become apparent from the study of a number of plant-pathogen interactions and those modelled by elicitor treatment of cultured cells that there may be more than one mechanism operating. However, one mechanism may be dominant in any given species. NADPH oxidases have been implicated in a number of systems and have been cloned and characterized. However, the enzyme system which is the major source of ROS in French bean (Phaseolus vulgaris) cells treated with a cell wall elicitor from Colletotrichum lindemuthianum, appears to be dependent on an exocellular peroxidase. The second component, the extracellular alkalinization, occurs as a result of the Ca(2+) and proton influxes and the K(+) efflux common to most elicitation systems as one of the earliest responses. The third component, the actual reductant/substrate, has remained elusive. The low molecular weight compound composition of apoplastic fluid was compared before and after elicitation. The substrate only becomes available some min after elicitation and can be extracted, so that by comparing the profiles by LC-MS it has been possible to identify possible substrates. The mechanism has proved to be complex and may involve a number of low molecular weight components. Stimulation of H(2)O(2) production was observed with saturated fatty acids such as palmitate and stearate without concomitant oxylipin production. This biochemical evidence is supported by immunolocalization studies on papillae forming at bacterial infection sites that show the peroxidase isoform present at sites of H(2)O(2) production revealed by cerium chloride staining together with the cross-linked wall proteins and callose and callose synthase. The peroxidase has been cloned and expressed in Pichia pastoris and has been shown to catalyse the oxidation reaction with the same kinetics as the purified enzyme. Furthermore, Arabidopsis plants transformed heterologously using the French bean peroxidase in antisense orientation have proved to be highly susceptible to bacterial and fungal pathogens. Thus it is possible that Arabidopsis is another species with the potential to mount an apoplastic oxidative burst and these transformed plant lines may be useful to identify the peroxidase that is responsible.
AuthorsG Paul Bolwell, Laurence V Bindschedler, Kristopher A Blee, Vernon S Butt, Dewi R Davies, Sarah L Gardner, Chris Gerrish, Farida Minibayeva
JournalJournal of experimental botany (J Exp Bot) Vol. 53 Issue 372 Pg. 1367-76 (May 2002) ISSN: 0022-0957 [Print] England
PMID11997382 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't, Review)
Chemical References
  • Fatty Acids
  • Reactive Oxygen Species
  • Hydrogen Peroxide
  • Peroxidase
Topics
  • Arabidopsis (genetics, metabolism, microbiology)
  • Colletotrichum (growth & development)
  • Fatty Acids (metabolism)
  • Gene Expression Regulation, Enzymologic
  • Gene Expression Regulation, Plant
  • Hydrogen Peroxide (metabolism)
  • Hydrogen-Ion Concentration
  • Oxidation-Reduction
  • Peroxidase (chemistry, genetics, metabolism)
  • Phaseolus (genetics, metabolism, microbiology)
  • Plant Diseases (microbiology)
  • Plants (genetics, metabolism, microbiology)
  • Protein Conformation
  • Reactive Oxygen Species (metabolism)
  • Signal Transduction

Join CureHunter, for free Research Interface BASIC access!

Take advantage of free CureHunter research engine access to explore the best drug and treatment options for any disease. Find out why thousands of doctors, pharma researchers and patient activists around the world use CureHunter every day.
Realize the full power of the drug-disease research graph!


Choose Username:
Email:
Password:
Verify Password:
Enter Code Shown: