The SseC translocon component in Salmonella enterica serovar Typhimurium is chaperoned by SscA

Cooper, Colin A.; Mulder, David T.; Allison, Sarah E.; Pilar, Ana Victoria C.; Coombes, Brian K.

doi:10.1186/1471-2180-13-221

Cited by 7 publications

(8 citation statements)

References 30 publications

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“…Although we detected only two virulence genes by KO classification, sopD and sseD , four other known virulence factors were up-regulated in low water activity conditions. These virulence factors included sscA , a chaperon for the SseC translocon [ 39 ]; sseA , a class II chaperone specific for translocon proteins SseB and SseD [ 40 – 42 ]; mviN , involved in peptidoglycan biosynthesis and required for virulence in mice [ 43 , 44 ]; and mgtC , part of the mgtBC operon in SPI-3, involved in the regulation of the membrane potential [ 45 ], and transcriptionally controlled by PhoP/PhoQ system [ 46 ].…”

Section: Resultsmentioning

confidence: 99%

“…SseD is a translocon component of the Salmonella Pathogenicity Island 2 (SPI-2) Type III Secretion System (T3SS) [ 66 ], and it is part of the sseABCD operon, encoding a chaperon protein and the other translocon components [ 67 ]. We also observed the induction of sseA , encoding the chaperonin for sseB and sseD [ 40 – 42 ], and sscA , encoding the chaperonin of sseC [ 39 ], in cells exposed to a w 0.11. This indicates that the entire SPI-2 T3SS translocon is likely involved during adaptation and survival to desiccation and low a w .…”

Section: Discussionmentioning

confidence: 99%

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General response of Salmonella enterica serovar Typhimurium to desiccation: A new role for the virulence factors sopD and sseD in survival

et al. 2017

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Salmonella can survive for long periods under extreme desiccation conditions. This stress tolerance poses a risk for food safety, but relatively little is known about the molecular and cellular regulation of this adaptation mechanism. To determine the genetic components involved in Salmonella’s cellular response to desiccation, we performed a global transcriptomic analysis comparing S. enterica serovar Typhimurium cells equilibrated to low water activity (aw 0.11) and cells equilibrated to high water activity (aw 1.0). The analysis revealed that 719 genes were differentially regulated between the two conditions, of which 290 genes were up-regulated at aw 0.11. Most of these genes were involved in metabolic pathways, transporter regulation, DNA replication/repair, transcription and translation, and, more importantly, virulence genes. Among these, we decided to focus on the role of sopD and sseD. Deletion mutants were created and their ability to survive desiccation and exposure to aw 0.11 was compared to the wild-type strain and to an E. coli O157:H7 strain. The sopD and sseD mutants exhibited significant cell viability reductions of 2.5 and 1.3 Log (CFU/g), respectively, compared to the wild-type after desiccation for 4 days on glass beads. Additional viability differences of the mutants were observed after exposure to aw 0.11 for 7 days. E. coli O157:H7 lost viability similarly to the mutants. Scanning electron microscopy showed that both mutants displayed a different morphology compared to the wild-type and differences in production of the extracellular matrix under the same conditions. These findings suggested that sopD and sseD are required for Salmonella’s survival during desiccation.

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Section: Resultsmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

General response of Salmonella enterica serovar Typhimurium to desiccation: A new role for the virulence factors sopD and sseD in survival

et al. 2017

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“…The second T3SS, encoded by SPI-2, translocates effector proteins into the host cell that are necessary for ensuring intracellular survival and replication (11,12). Chaperone-effector interactions have been charted extensively for both the T3SS-1 (13-16) and T3SS-2 (17)(18)(19)(20)(21)(22), and a number of functions attributed to secretion chaperones beyond that of effector binding have been demonstrated in Salmonella (23,24).…”

mentioning

confidence: 99%

Identification of the Docking Site between a Type III Secretion System ATPase and a Chaperone for Effector Cargo

Allison

Tuinema

Everson

et al. 2014

Journal of Biological Chemistry

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Background: Chaperones engage type III secretion system (T3SS) ATPases to facilitate effector secretion. Results: The molecular basis of the chaperone-T3SS ATPase interaction interface was elucidated. Conclusion: The C-terminal region of T3SS ATPases mediates binding with multiple contact points along the chaperone. Significance: The chaperone-T3SS ATPase interaction is important for Salmonella pathogenesis and may be a target for anti-virulence drugs.

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“…A ΔespD strain secretes decreased protein level of EspA, an EseB homologue (35.2% similarity) (5,25). Also, deletion of YopB or SseC does not affect the secretion of EseD homologues YopD or SseD (5,26,27). Thus, the means by which EseC controls EseB/D secretion seems be unique to E. piscicida.…”

Section: Discussionmentioning

confidence: 98%

The Edwardsiella piscicida Type III Translocon Protein EseC Inhibits Biofilm Formation by Sequestering EseE

Liu

et al. 2019

Appl Environ Microbiol

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The type III secretion system (T3SS) is one of the most important virulence factors of the fish pathogen Edwardsiella piscicida. It contains three translocon proteins, EseB, EseC, and EseD, required for translocation of effector proteins into host cells. We have previously shown that EseB forms filamentous appendages on the surface of E. piscicida, and these filamentous structures mediate bacterial cell-cell interactions promoting autoaggregation and biofilm formation. In the present study, we show that EseC, but not EseD, inhibits the autoaggregation and biofilm formation of E. piscicida. At 18 h postsubculture, a ΔeseC strain developed strong autoaggregation and mature biofilm formation, accompanied by enhanced formation of EseB filamentous appendages. This is in contrast to the weak autoaggregation and immature biofilm formation seen in the E. piscicida wild-type strain. EseE, a protein that directly binds to EseC and also positively regulates the transcription of the escC-eseE operon, was liberated and showed increased levels in the absence of EseC. This led to augmented transcription of the escC-eseE operon, thereby increasing the steady-state protein levels of intracellular EseB, EseD, and EseE, as well as biofilm formation. Notably, the levels of intracellular EseB and EseD produced by the ΔeseE and ΔeseC ΔeseE strains were similar but remarkably lower than those produced by the wild-type strain at 18 h postsubculture. Taken together, we have shown that the translocon protein EseC inhibits biofilm formation through sequestering EseE, a positive regulator of the escC-eseE operon. IMPORTANCE Edwardsiella piscicida, previously known as Edwardsiella tarda, is a Gram-negative intracellular pathogen that mainly infects fish. The type III secretion system (T3SS) plays a pivotal role in its pathogenesis. The T3SS translocon protein EseB is required for the assembly of filamentous appendages on the surface of E. piscicida. The interactions between the appendages facilitate autoaggregation and biofilm formation. In this study, we explored the role of the other two translocon proteins, EseC and EseD, in biofilm formation. We have demonstrated that EseC, but not EseD, inhibits the autoaggregation and biofilm formation of E. piscicida, providing new insights into the regulatory mechanism involved in E. piscicida biofilm formation.

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The SseC translocon component in Salmonella enterica serovar Typhimurium is chaperoned by SscA

Cited by 7 publications

References 30 publications

General response of Salmonella enterica serovar Typhimurium to desiccation: A new role for the virulence factors sopD and sseD in survival

General response of Salmonella enterica serovar Typhimurium to desiccation: A new role for the virulence factors sopD and sseD in survival

Identification of the Docking Site between a Type III Secretion System ATPase and a Chaperone for Effector Cargo

The Edwardsiella piscicida Type III Translocon Protein EseC Inhibits Biofilm Formation by Sequestering EseE

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