The Salmonella Type III Secretion System Virulence Effector Forms a New Hexameric Chaperone Assembly for Export of Effector/Chaperone Complexes

Tsai, Chi Lin; Burkinshaw, Brianne J.; Strynadka, N.C.J.; Tainer, John A.

doi:10.1128/jb.02524-14

Cited by 12 publications

(9 citation statements)

References 33 publications

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“…However, monitoring bacterial effector proteins during the infection of live cells is technically challenging due to the mechanism of effector protein translocation through the T3SS into the host cell. Effector proteins are escorted and unfolded by chaperones in the bacterial cytosol in order to be threaded through the needle-like T3SS translocon for transport into the host cell, where the effectors are then refolded following delivery into the host cytosol (Akeda and Galán, 2005 ; Tsai et al, 2015 ). This process of threading through the translocon is incompatible with fluorescent protein (FP) tagging due to the high thermodynamic stability of FPs (Radics et al, 2014 ).…”

Section: Live Cell Methods To Visualize Effector Proteins In Host Celmentioning

confidence: 99%

Methods to Illuminate the Role of Salmonella Effector Proteins during Infection: A Review

Young

Palmer

2017

Front. Cell. Infect. Microbiol.

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Intracellular bacterial pathogens like Salmonella enterica use secretion systems, such as the Type III Secretion System, to deliver virulence factors into host cells in order to invade and colonize these cells. Salmonella virulence factors include a suite of effector proteins that remodel the host cell to facilitate bacterial internalization, replication, and evasion of host immune surveillance. A number of diverse and innovative approaches have been used to identify and characterize the role of effector proteins during infection. Recent techniques for studying infection using single cell and animal models have illuminated the contribution of individual effector proteins in infection. This review will highlight the techniques applied to study Salmonella effector proteins during infection. It will describe how different approaches have revealed mechanistic details for effectors in manipulating host cellular processes including: the dynamics of effector translocation into host cells, cytoskeleton reorganization, membrane trafficking, gene regulation, and autophagy.

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Section: Live Cell Methods To Visualize Effector Proteins In Host Celmentioning

confidence: 99%

Methods to Illuminate the Role of Salmonella Effector Proteins during Infection: A Review

Young

Palmer

2017

Front. Cell. Infect. Microbiol.

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“…Another way to characterise this complex apparatus is based on the location of the different proteins. This allows dividing the T3SS into three regions: the cytoplasmic region, the trans-membrane region, also known as the basal body [ 21 ], and the extra-cellular region (Figure 2 ). The main role of the cytoplasmic region is to interact with proteins in the bacterial cytoplasm and to recruit effector proteins before directing them to the rest of the secretory apparatus.…”

Section: The T3ssmentioning

confidence: 99%

Delivering the pain: an overview of the type III secretion system with special consideration for aquatic pathogens

Rahmatelahi

El‐Matbouli

Menanteau–Ledouble

2021

Vet Res

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Gram-negative bacteria are known to subvert eukaryotic cell physiological mechanisms using a wide array of virulence factors, among which the type three-secretion system (T3SS) is often one of the most important. The T3SS constitutes a needle-like apparatus that the bacterium uses to inject a diverse set of effector proteins directly into the cytoplasm of the host cells where they can hamper the host cellular machinery for a variety of purposes. While the structure of the T3SS is somewhat conserved and well described, effector proteins are much more diverse and specific for each pathogen. The T3SS can remodel the cytoskeleton integrity to promote intracellular invasion, as well as silence specific eukaryotic cell signals, notably to hinder or elude the immune response and cause apoptosis. This is also the case in aquatic bacterial pathogens where the T3SS can often play a central role in the establishment of disease, although it remains understudied in several species of important fish pathogens, notably in Yersinia ruckeri. In the present review, we summarise what is known of the T3SS, with a special focus on aquatic pathogens and suggest some possible avenues for research including the potential to target the T3SS for the development of new anti-virulence drugs.

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“…The band was restored when the wild type IpgE chaperone was expressed on a plasmid. It was hypothesized that chaperones maintain an extended conformation of the N-terminus of effectors before they are translocated [47,48,62].…”

Section: Protein Foldingmentioning

confidence: 99%

Delivery of Heterologous Proteins, Enzymes, and Antigens via the Bacterial Type III Secretion System

Pendergrass

May

2020

Microorganisms

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The Type III Secretion System (T3SS) is a multimeric protein complex composed of over 20 different proteins, utilized by Gram-negative bacteria to infect eukaryotic host cells. The T3SS has been implicated as a virulence factor by which pathogens cause infection and has recently been characterized as a communication tool between bacteria and plant cells in the rhizosphere. The T3SS has been repurposed to be used as a tool for the delivery of non-native or heterologous proteins to eukaryotic cells or the extracellular space for a variety of purposes, including drug discovery and drug delivery. This review covers the methodology of heterologous protein secretion as well as multiple cases of utilizing the T3SS to deliver heterologous proteins or artificial materials. The research covered in this review will serve to outline the scope and limitations of utilizing the T3SS as a tool for protein delivery.

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The Salmonella Type III Secretion System Virulence Effector Forms a New Hexameric Chaperone Assembly for Export of Effector/Chaperone Complexes

Abstract: -14) show that the T3SS chaperone SigE of Salmonella can form hexameric rings rather than dimers when bound to its cognate effector, SopB, implying a novel multimeric association for chaperone/effector complexes with their ATPase.

Cited by 12 publications

References 33 publications

Methods to Illuminate the Role of Salmonella Effector Proteins during Infection: A Review

Methods to Illuminate the Role of Salmonella Effector Proteins during Infection: A Review

Delivering the pain: an overview of the type III secretion system with special consideration for aquatic pathogens

Delivery of Heterologous Proteins, Enzymes, and Antigens via the Bacterial Type III Secretion System

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