Proteomics

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The periplasmic oxidoreductase DsbA is required for virulence of the phytopathogen Dickeya solani


ABSTRACT: The DsbA oxidoreductase is a crucial factor responsible for introduction of disulfide bonds to the extracytoplasmic proteins in bacteria. A lack of the proper disulfides frequently leads to instability and/or loss of protein function. In pathogens, numerous envelope and extracellular proteins play important roles in pathogenesis; therefore, their improper disulfide bonding may lead to avirulent phenotypes. The importance of the DsbA function in phytopathogens has not been extensively studied yet. Dickeya solani is a bacterium from the Soft Rot Pectobacteriaceae group which is responsible for very high economic losses mainly on potato. In recent years, D. solani became the most abundant potato pathogen among Dickeya species in Europe. In this work, using the D. solani dsbA mutant, we demonstrated that a lack of the DsbA function caused loss of virulence. Mutant bacteria were deficient in most secreted virulence determinants and were not able to develop disease symptoms in the natural host, the potato plant. The SWATH-MS-based proteomic analysis revealed that the dbsA mutation led to multifaceted effects in the D. solani cells. First of all, the levels of the majority of plant cell wall degrading enzymes and proteins related to motility and chemotaxis were severely reduced. Furthermore, the protein profiles suggested induction of the envelope and cytoplasm stress responses in the mutant cells. Finally, the outer membrane barrier seemed to be disturbed by the mutation. Our results clearly demonstrate that the function played by the DsbA oxidoreductase is indispensable for D. solani virulence and a lack of DsbA significantly disturbs cellular physiology. A thorough analysis of proteomic research suggests that a lack of virulence may result from both, abnormalities of the disulfide deprived virulence determinants and the envelope stress-dependent repression of the virulence genes in the dsbA mutant.

INSTRUMENT(S): TripleTOF 5600+

ORGANISM(S): Dickeya Solani

SUBMITTER: Aleksandra Bogucka  

LAB HEAD: Paulina Czaplewska

PROVIDER: PXD028047 | Pride | 2022-02-15

REPOSITORIES: pride

Dataset's files

Source:
Action DRS
checksum.txt Txt
d_solani_proteome.group Other
d_solani_secretome_lib.group Other
proteome-library.zip Other
proteome-swath.zip Other
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Publications

The Periplasmic Oxidoreductase DsbA Is Required for Virulence of the Phytopathogen <i>Dickeya solani</i>.

Przepiora Tomasz T   Figaj Donata D   Bogucka Aleksandra A   Fikowicz-Krosko Jakub J   Czajkowski Robert R   Hugouvieux-Cotte-Pattat Nicole N   Skorko-Glonek Joanna J  

International journal of molecular sciences 20220109 2


In bacteria, the DsbA oxidoreductase is a crucial factor responsible for the introduction of disulfide bonds to extracytoplasmic proteins, which include important virulence factors. A lack of proper disulfide bonds frequently leads to instability and/or loss of protein function; therefore, improper disulfide bonding may lead to avirulent phenotypes. The importance of the DsbA function in phytopathogens has not been extensively studied yet. <i>Dickeya solani</i> is a bacterium from the Soft Rot <  ...[more]

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