Title
Proteomic profiling of cellular targets of lipopolysaccharide-induced signalling in Nicotiana tabacum BY-2 cellsProteomic profiling of cellular targets of lipopolysaccharide-induced signalling in Nicotiana tabacum BY-2 cells
Author
Faculty/Department
Faculty of Sciences. Biology
Faculty of Sciences. Chemistry
Faculty of Sciences. Mathematics and Computer Science
Research group
Integrated Molecular Plant Physiology Research (IMPRES)
Systemic Physiological and Ecotoxicological Research (SPHERE)
Algebra, geometry and ISLAb
Biomolecular & Analytical Mass Spectrometry (BAMS)
Publication type
article
Publication
Amsterdam,
Subject
Biology
Source (journal)
Biochimica et biophysica acta : proteins and proteomics. - Amsterdam
Volume/pages
1784(2008):11, p. 1750-1762
ISSN
1570-9639
ISI
000261019000033
Carrier
E
Target language
English (eng)
Full text (Publishers DOI)
Affiliation
University of Antwerp
Abstract
Plants constantly monitor for pathogen challenge and utilize a diverse array of adaptive defense mechanisms, including differential protein regulation, during pathogen attack. A proteomic analysis of Nicotiana tabacum BY-2 cells was performed in order to investigate the dynamic changes following perception of bacterial lipopolysaccharides. A multiplexed proteome analysis, employing two-dimensional difference-in-gel-electrophoresis with CyDye DIGE fluors, as well as Ruthenium II tris (bathophenanthroline disulfonate) fluorescence staining and Pro-Q® Diamond phosphoprotein-specific gel staining, monitored over 1500 proteins and resulted in the identification of 88 differentially regulated proteins and phosphoproteins responsive to LPSB.cep.-elicitation. Functional clustering of the proteins both at the level of their abundance and phosphorylation status, revealed 9 proteins involved in transport, ion homeostasis and signal transduction. A large number of responsive proteins were found to be involved in metabolism- and energy-related processes (36), representing various metabolic pathways. Another abundant category corresponded to proteins classified as molecular chaperones and involved in protein destination/targeting (12). Other categories of proteins found to be LPSB.cep.-responsive and differentially regulated include cell structure- and cytoskeletal rearrangement proteins (8) and proteins involved in transcription and translation as well as degradation (11). The results indicate that LPSB.cep. induces metabolic reprogramming and changes in cellular activities supporting protein synthesis, -folding, vesicle trafficking and secretion; accompanied by changes to the cytoskeleton and proteosome function. Many of the identified proteins are known to be interconnected at various levels through a complex web of activation/deactivation, complex formation, proteinprotein interactions, and chaperoning reactions. The presented data offers novel insights and further evidence for the biochemical action of LPSB.cep. as a resistance elicitor, a pathogen-associated molecular pattern molecule and triggering agent of defense responses associated with innate immunity.
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