scholarly journals EssC is a specificity determinant for Staphylococcus aureus type VII secretion

2018 ◽  
Author(s):  
Franziska Jäger ◽  
Holger Kneuper ◽  
Tracy Palmer
Keyword(s):  
Staphylococcus Aureus ◽  
Protein Secretion ◽  
Secretion System ◽  
Sequence Variability ◽  
Display Sequence ◽  
Type Vii Secretion ◽  
Substrate Protein ◽  
Protein Secretion System ◽  
Membrane Bound ◽  
Substrate Proteins

ABSTRACTThe Type VII protein secretion system (T7SS) is found in actinobacteria and firmicutes, and plays important roles in virulence and interbacterial competition. A membrane-bound ATPase protein, EssC in Staphylococcus aureus, lies at the heart of the secretion machinery. The EssC protein from S. aureus strains can be grouped into four variants (EssC1-EssC4) that display sequence variability in the C-terminal region. Here we show that the EssC2, EssC3 and EssC4 variants can be produced in a strain deleted for essC1 and that they are able to mediate secretion of EsxA, an essential component of the secretion apparatus. They are, however, unable to support secretion of the substrate protein EsxC, which is encoded only in essC1-specific strains. This finding indicates that EssC is a specificity determinant for T7 protein secretion. Our results support a model where the C-terminal domain of EssC interacts with substrate proteins whereas EsxA interacts elsewhere.

scholarly journals A membrane-depolarizing toxin substrate of theStaphylococcus aureustype VII secretion system mediates intraspecies competition

2020 ◽  
Vol 117 (34) ◽  
pp. 20836-20847 ◽  
Author(s):  
Fatima R. Ulhuq ◽  
Margarida C. Gomes ◽  
Gina M. Duggan ◽  
Manman Guo ◽  
Chriselle Mendonca ◽  
...  
Keyword(s):  
Secretion System ◽  
Infection Model ◽  
Substrate Protein ◽  
Proteomic Approach ◽  
Protein Secretion System ◽  
Membrane Bound ◽  
Intraspecies Competition ◽  
Dependent Growth ◽  
Bacterial Replication

The type VII protein secretion system (T7SS) is conserved acrossStaphylococcus aureusstrains and plays important roles in virulence and interbacterial competition. To date, only one T7SS substrate protein, encoded in a subset ofS. aureusgenomes, has been functionally characterized. Here, using an unbiased proteomic approach, we identify TspA as a further T7SS substrate. TspA is encoded distantly from the T7SS gene cluster and is found across allS. aureusstrains as well as inListeriaand Enterococci. Heterologous expression of TspA fromS. aureusstrain RN6390 indicates its C-terminal domain is toxic when targeted to theEscherichia coliperiplasm and that it depolarizes the cytoplasmic membrane. The membrane-depolarizing activity is alleviated by coproduction of the membrane-bound TsaI immunity protein, which is encoded adjacent totspAon theS. aureuschromosome. Using a zebrafish hindbrain ventricle infection model, we demonstrate that the T7SS of strain RN6390 promotes bacterial replication in vivo, and deletion oftspAleads to increased bacterial clearance. The toxin domain of TspA is highly polymorphic andS. aureusstrains encode multipletsaIhomologs at thetspAlocus, suggestive of additional roles in intraspecies competition. In agreement, we demonstrate TspA-dependent growth inhibition of RN6390 by strain COL in the zebrafish infection model that is alleviated by the presence of TsaI homologs.

scholarly journals A holin/peptidoglycan hydrolase‐dependent protein secretion system

2020 ◽  
Author(s):  
Tracy Palmer ◽  
Alexander J. Finney ◽  
Chayan Kumar Saha ◽  
Gemma C. Atkinson ◽  
Frank Sargent
Keyword(s):  
Protein Secretion ◽  
Secretion System ◽  
Peptidoglycan Hydrolase ◽  
Protein Secretion System ◽  
Dependent Protein

scholarly journals Genomewide identification of proteins secreted by the Hrp type III protein secretion system of Pseudomonas syringae pv. tomato DC3000

2002 ◽  
Vol 99 (11) ◽  
pp. 7652-7657 ◽  
Author(s):  
T. Petnicki-Ocwieja ◽  
D. J. Schneider ◽  
V. C. Tam ◽  
S. T. Chancey ◽  
L. Shan ◽  
...  
Keyword(s):  
Pseudomonas Syringae ◽  
Protein Secretion ◽  
Secretion System ◽  
Tomato Dc3000 ◽  
Type Iii ◽  
Protein Secretion System ◽  
Type Iii Protein Secretion

scholarly journals PopF1 and PopF2, Two Proteins Secreted by the Type III Protein Secretion System of Ralstonia solanacearum, Are Translocators Belonging to the HrpF/NopX Family

2006 ◽  
Vol 188 (13) ◽  
pp. 4903-4917 ◽  
Author(s):  
Damien Meyer ◽  
Sébastien Cunnac ◽  
Mareva Guéneron ◽  
Céline Declercq ◽  
Frédérique Van Gijsegem ◽  
...  
Keyword(s):  
Protein Secretion ◽  
Ralstonia Solanacearum ◽  
Xanthomonas Campestris ◽  
Pathogenic Bacteria ◽  
Secretion System ◽  
Effector Proteins ◽  
Experimental Conditions ◽  
Type Iii ◽  
Protein Secretion System ◽  
Type Iii Protein Secretion

ABSTRACT Ralstonia solanacearum GMI1000 is a gram-negative plant pathogen which contains an hrp gene cluster which codes for a type III protein secretion system (TTSS). We identified two novel Hrp-secreted proteins, called PopF1 and PopF2, which display similarity to one another and to putative TTSS translocators, HrpF and NopX, from Xanthomonas spp. and rhizobia, respectively. They also show similarities with TTSS translocators of the YopB family from animal-pathogenic bacteria. Both popF1 and popF2 belong to the HrpB regulon and are required for the interaction with plants, but PopF1 seems to play a more important role in virulence and hypersensitive response (HR) elicitation than PopF2 under our experimental conditions. PopF1 and PopF2 are not necessary for the secretion of effector proteins, but they are required for the translocation of AvrA avirulence protein into tobacco cells. We conclude that PopF1 and PopF2 are type III translocators belonging to the HrpF/NopX family. The hrpF gene of Xanthomonas campestris pv. campestris partially restored HR-inducing ability to popF1 popF2 mutants of R. solanacearum, suggesting that translocators of R. solanacearum and Xanthomonas are functionally conserved. Finally, R. solanacearum strain UW551, which does not belong to the same phylotype as GMI1000, also possesses two putative translocator proteins. However, although one of these proteins is clearly related to PopF1 and PopF2, the other seems to be different and related to NopX proteins, thus showing that translocators might be variable in R. solanacearum.

scholarly journals The Ess/Type VII secretion system of Staphylococcus aureus shows unexpected genetic diversity

BMC Genomics ◽  
2016 ◽  
Vol 17 (1) ◽  
Author(s):  
Ben Warne ◽  
Catriona P. Harkins ◽  
Simon R. Harris ◽  
Alexandra Vatsiou ◽  
Nicola Stanley-Wall ◽  
...  
Keyword(s):  
Genetic Diversity ◽  
Staphylococcus Aureus ◽  
Secretion System ◽  
Type Vii Secretion ◽  
Type Vii Secretion System

scholarly journals ClpXP Protease Controls Expression of the Type III Protein Secretion System through Regulation of RpoS and GrlR Levels in Enterohemorrhagic Escherichia coli

2005 ◽  
Vol 187 (12) ◽  
pp. 4086-4094 ◽  
Author(s):  
Sunao Iyoda ◽  
Haruo Watanabe
Keyword(s):  
Escherichia Coli ◽  
Protein Secretion ◽  
Deletion Mutant ◽  
Regulatory Gene ◽  
Secretion System ◽  
Enterohemorrhagic Escherichia Coli ◽  
Multicopy Plasmid ◽  
Type Iii ◽  
Protein Secretion System ◽  
Type Iii Protein Secretion

ABSTRACT Expression of the type III protein secretion system (TTSS), encoded in the locus of enterocyte effacement (LEE) of enterohemorrhagic Escherichia coli (EHEC), has been shown to be controlled by various regulators. In a search for additional regulatory genes, we identified a DNA fragment containing clpX and clpP that has a positive regulatory effect on LEE expression in EHEC O157. The expression of LEE-encoded Esp proteins was significantly reduced in a clpXP deletion mutant. Deletion of grlR, a negative regulatory gene within LEE, markedly increased LEE expression even in the clpXP mutant. To verify the regulatory mechanism of GrlR expression, a chromosomal epitope-tagged allele of grlR (grlR-FLAG) was constructed. GrlR-FLAG expression was increased significantly in the clpXP deletion mutant, suggesting that the GrlR level is under the control of ClpXP, and this regulation is critical for the ClpXP-dependent expression of LEE in EHEC. Deletion of rpoS, the gene encoding a stationary-phase-inducing sigma factor that is a substrate for ClpXP protease, partially restored LEE expression in the clpXP mutant. A multicopy plasmid carrying rpoS strongly repressed expression of Esp proteins, suggesting that positive regulation by ClpXP is partially mediated through a negative effect of RpoS on LEE expression. We also found that rpoS deletion induces transcription of pchA, which encodes one of the positive regulators for LEE expression in EHEC. These results suggest that ClpXP controls expression of LEE through the regulation of RpoS and GrlR levels in EHEC.

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