Proteomic analysis of a non-virulent mutant of the phytopathogenic bacterium Erwinia chrysanthemi deficient in osmoregulated periplasmic glucans: change in protein expression is not restricted to the envelope, but affects general metabolism

Bouchart, Franck; Delangle, Aurélie; Lemoine, Jérôme; Bohin, Jean-Pierre; Lacroix, Jean-Marie

doi:10.1099/mic.0.2006/000372-0

Cited by 31 publications

(27 citation statements)

References 29 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…(37,38), reduce flagella assembly, and increase sensitivity to antibiotics and detergents (in Rhizobium and Agrobacterium sp and P. aeruginosa) (4,39,40), and to have pleiotropic effects on polysaccharide biosynthesis, protein folding and degradation, and carbohydrate catabolism (in Erwinia chrysanthemi) (41). Loss of periplasmic glucan production in R. meliloti and Bradyrhizobium japonicum affected growth in various hypoosmotic environments (42,43), whereas the opposite effect, decreased growth rates in a hyperosmotic high sodium chloride environment was observed for the C. jejuni pglB, pglE, and pglF mutants where no detectable fOS was present.…”

Section: Discussionmentioning

confidence: 99%

Study of free oligosaccharides derived from the bacterial N -glycosylation pathway

Nothaft

Liu

McNally

et al. 2009

Proc. Natl. Acad. Sci. U.S.A.

View full text Add to dashboard Cite

The food-borne pathogen Campylobacter jejuni is one of the leading causes of bacterial gastroenteritis worldwide and the most frequent antecedent in neuropathies such as the Guillain-Barré and Miller Fisher syndromes. C. jejuni was demonstrated to possess an N-linked protein glycosylation pathway that adds a conserved heptasaccharide to >40 periplasmic and membrane proteins. Recently, we showed that C. jejuni also produces free heptasaccharides derived from the N-glycan pathway reminiscent of the free oligosaccharides (fOS) produced by eukaryotes. Herein, we demonstrate that C. jejuni fOS are produced in response to changes in the osmolarity of the environment and bacterial growth phase. We provide evidence showing the conserved WWDYG motif of the oligosaccharyltransferase, PglB, is necessary for fOS release into the periplasm. This report demonstrates that fOS from an N-glycosylation pathway in bacteria are potentially equivalent to osmoregulated periplasmic glucans in other Gram-negative organisms.Campylobacter jejuni ͉ N-linked protein glycosylation ͉ periplasmic glucans ͉ osmolarity

show abstract

Section: Discussionmentioning

confidence: 99%

Study of free oligosaccharides derived from the bacterial N -glycosylation pathway

Nothaft

Liu

McNally

et al. 2009

Proc. Natl. Acad. Sci. U.S.A.

View full text Add to dashboard Cite

show abstract

“…The extracytoplasmic stress may be of various types and may involve signal transduction pathways such as RpoE, CpxAR, BaeRS, Rcs (phosphorelays), or PSP (phage shock response) (43,57,58,60,61). In fact, activation of both the RpoE and Rcs phosphorelay systems has been observed in rfa mutants as well as in MDO-, SurA-, and Tol-deficient strains (8,12,19,43,52,78), and induction of oxidative stress has been reported for waaL mutants (5). In addition, inactivation of SurA, a periplasmic chaperone required for outer membrane protein biogenesis (67), results in increased sensitivity to iron (72), again suggesting that cell envelope perturbation leads to oxidative stress.…”

Section: Vol 191 2009 T2s System Iron Homeostasis and Stress Respmentioning

confidence: 99%

Cell Envelope Perturbation Induces Oxidative Stress and Changes in Iron Homeostasis inVibrio cholerae

et al. 2009

View full text Add to dashboard Cite

The Vibrio cholerae type II secretion (T2S) machinery is a multiprotein complex that spans the cell envelope. When the T2S system is inactivated, cholera toxin and other exoproteins accumulate in the periplasmic compartment. Additionally, loss of secretion via the T2S system leads to a reduced growth rate, compromised outer membrane integrity, and induction of the extracytoplasmic stress factor RpoE (A. E. Sikora, S. R. Lybarger, and M. Sandkvist, J. Bacteriol. 189:8484-8495, 2007). In this study, gene expression profiling reveals that inactivation of the T2S system alters the expression of genes encoding cell envelope components and proteins involved in central metabolism, chemotaxis, motility, oxidative stress, and iron storage and acquisition. Consistent with the gene expression data, molecular and biochemical analyses indicate that the T2S mutants suffer from internal oxidative stress and increased levels of intracellular ferrous iron. By using a tolA mutant of V. cholerae that shares a similar compromised membrane phenotype but maintains a functional T2S machinery, we show that the formation of radical oxygen species, induction of oxidative stress, and changes in iron physiology are likely general responses to cell envelope damage and are not unique to T2S mutants. Finally, we demonstrate that disruption of the V. cholerae cell envelope by chemical treatment with polymyxin B similarly results in induction of the RpoE-mediated stress response, increased sensitivity to oxidants, and a change in iron metabolism. We propose that many types of extracytoplasmic stresses, caused either by genetic alterations of outer membrane constituents or by chemical or physical damage to the cell envelope, induce common signaling pathways that ultimately lead to internal oxidative stress and misregulation of iron homeostasis.Vibrio cholerae, a rod-shaped, highly motile, gram-negative bacterium, is the causative agent of the life threatening diarrheal disease cholera (59). The type II secretion (T2S) system plays an important role in the pathogenesis of V. cholerae by secreting cholera toxin (63), which is largely responsible for the symptoms of the disease (33). The T2S system is widespread and well conserved in gram-negative bacteria inhabiting a variety of ecological niches and likely contributes to environmental survival as well as to virulence (11,21). In V. cholerae, secretion via the T2S machinery is supported by a transenvelope complex of 12 Eps proteins (EpsC to EpsN) and the type 4 prepilin peptidase PilD (VcpD) (25,44,63). Transport of exoproteins by the T2S system occurs via a two-step process. The first step, which is either Sec or Tat dependent, requires recognition of the N-terminal signal peptide of the exoproteins and translocation through the inner membrane to the periplasm. Then the folded proteins engage the T2S machinery and are subsequently exported across the outer membrane to the extracellular milieu (23,29).Besides periplasmic accumulation of exoproteins, additional phenotypes of T2S mutants are reporte...

show abstract

“…Second, in E. coli, it was shown that closing of the tricarboxylic acid (TCA) cycle generated ROS synthesis within bacteria, thus inducing the ROS stress response (Kohanski et al, 2008), and in a previous proteomic analysis (Bouchart et al, 2007), it was shown that in an opgG strain, increasing energy level was required as compared with a wild-type strain and resulted in a closed TCA cycle. To test these hypotheses, an opgG eps double mutant strain was constructed by transduction.…”

Section: Motility Is Not Restored In the Opgg Pecs Double Mutant Strainmentioning

confidence: 99%

“…In D. dadantii, mutants devoid of OPGs show a pleiotropic phenotype including a loss of motility, decreased synthesis and secretion of PCWDEs linked to reduced synthesis of the Out system, increased synthesis of exopolysaccharide, induction of a general stress response and complete loss of virulence on potato tubers or chicory leaves (Bouchart et al, 2007;Page et al, 2001). In strains of D. dadantii devoid of OPGs, inactivation of the RcsCDB phosphorelay regulatory system restored PCWDE synthesis and secretion, motility, normal exopolysaccharide synthesis and virulence in potato tubers, indicating that OPGs control the activation level of this phosphorelay (Bontemps-Gallo et al, 2013;Bouchart et al, 2010).…”

Section: Introductionmentioning

confidence: 99%

Inactivation of pecS restores the virulence of mutants devoid of osmoregulated periplasmic glucans in the phytopathogenic bacterium Dickeya dadantii

2014

View full text Add to dashboard Cite

Dickeya dadantii is a phytopathogenic enterobacterium that causes soft rot disease in a wide range of plant species. Maceration, an apparent symptom of the disease, is the result of the synthesis and secretion of a set of plant cell wall-degrading enzymes (PCWDEs), but many additional factors are required for full virulence. Among these, osmoregulated periplasmic glucans (OPGs) and the PecS transcriptional regulator are essential virulence factors. Several cellular functions are controlled by both OPGs and PecS. Strains devoid of OPGs display a pleiotropic phenotype including total loss of virulence, loss of motility and severe reduction in the synthesis of PCWDEs. PecS is one of the major regulators of virulence in D. dadantii, acting mainly as a repressor of various cellular functions including virulence, motility and synthesis of PCWDEs. The present study shows that inactivation of the pecS gene restored virulence in a D. dadantii strain devoid of OPGs, indicating that PecS cannot be de-repressed in strains devoid of OPGs.

show abstract

Proteomic analysis of a non-virulent mutant of the phytopathogenic bacterium Erwinia chrysanthemi deficient in osmoregulated periplasmic glucans: change in protein expression is not restricted to the envelope, but affects general metabolism

Cited by 31 publications

References 29 publications

Study of free oligosaccharides derived from the bacterial N -glycosylation pathway

Study of free oligosaccharides derived from the bacterial N -glycosylation pathway

Cell Envelope Perturbation Induces Oxidative Stress and Changes in Iron Homeostasis inVibrio cholerae

Inactivation of pecS restores the virulence of mutants devoid of osmoregulated periplasmic glucans in the phytopathogenic bacterium Dickeya dadantii

Contact Info

Product

Resources

About