A Sorting Platform Determines the Order of Protein Secretion in Bacterial Type III Systems

Lara‐Tejero, María; Kato, Junya; Wagner, Samuel; Liu, Xiaoyun; Galán, Jorge E.

doi:10.1126/science.1201476

Cited by 241 publications

(325 citation statements)

References 35 publications

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“…It has been previously shown that there is a hierarchy in the type III secretion process so that different proteins are engaged at different times (10,29). Proteins necessary for the assembly of the needle and inner rod substructures of the needle complex are engaged first.…”

Section: Prgj Mutant Strains With Aberrant Needle Length Are Able To mentioning

confidence: 99%

“…However, the hierarchy in the secretion process extends beyond needle complex assembly because the protein translocases, which mediate the passage of effectors through the target host cell membrane, must be secreted before the effector proteins themselves. Indeed, a cytoplasmic sorting platform has been shown to be critical to the establishment of the secretion hierarchy (10). We examined the PrgJ mutants for their ability to secrete proteins within the different hierarchical categories of type III secretion.…”

Section: Prgj Mutant Strains With Aberrant Needle Length Are Able To mentioning

confidence: 99%

“…TTSSs consist of the envelope-associated needle complex, which mediates the passage of the secreted proteins through the bacterial envelope, and several cytoplasmic accessory proteins, which are required for the recognition and sorting of the proteins destined to travel this pathway (5,6,9,10). The needle complex is composed of a multiring, envelope-associated base substructure, and a filament or needle seated on the base, projecting outward from the bacterial surface (9,11).…”

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The inner rod protein controls substrate switching and needle length in a Salmonella type III secretion system

Lefebre

Galán

2013

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

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Type III secretion machines are essential for the biology of many bacteria that are pathogenic or symbiotic for animals, plants, or insects. They exert their function by delivering bacterial effector proteins into target eukaryotic cells. The core component of these machines is the needle complex, a multiprotein structure that spans the bacterial envelope and serves as a conduit for proteins that transit this secretion pathway. The needle complex is composed of a multiring base embedded in the bacterial envelope and a filament-like structure, the needle, that projects from the bacterial surface and is linked to the base by the inner rod. Assembly of the needle complex proceeds in a step-wise fashion that is initiated by the assembly of the base and is followed by the export of the building subunits for the needle and inner rod substructures. Once assembled, the needle complex reprograms its specificity and becomes competent for the secretion of effector proteins. Here through genetic, biochemical, and electron microscopy analyses of the Salmonella inner rod protein subunit PrgJ we present evidence that the assembly of the inner rod dictates the timing of substrate switching and needle length. Furthermore, the identification of mutations in PrgJ that specifically alter the hierarchy of protein secretion provides additional support for a complex role of the inner rod substructure in type III secretion.bacterial pathogenesis | organelle assembly | Salmonella pathogenesis

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Section: Prgj Mutant Strains With Aberrant Needle Length Are Able To mentioning

confidence: 99%

Section: Prgj Mutant Strains With Aberrant Needle Length Are Able To mentioning

confidence: 99%

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confidence: 99%

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The inner rod protein controls substrate switching and needle length in a Salmonella type III secretion system

Lefebre

Galán

2013

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

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“…During infection of vertebrate cells, the protozoan pathogen Toxoplasma gondii secretes effectors by sequential triggering of three distinct parasite organelles known as micronemes, rhoptries, and dense granules, at different phases during its intracellular growth (Carruthers and Sibley 1997). Bacterial enteropathogen Salmonella enterica uses a sorting platform involving chaperone proteins to sort and load the effectors to be secreted in a defined order via T3SS (Lara-Tejero et al 2011). In bacterial plant pathogens, T3SS is also used to deliver effectors into plant cells in a regulated manner.…”

Section: Temporal Aspects Of Pathogen Deployment Of Effectorsmentioning

confidence: 99%

Effector Biology of Plant-Associated Organisms: Concepts and Perspectives

Win

Chaparro-Garcia

Belhaj

et al. 2012

Cold Spring Harbor Symposia on Quantitative Biology

350

329

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Every plant is closely associated with a variety of living organisms. Therefore, deciphering how plants interact with mutualistic and parasitic organisms is essential for a comprehensive understanding of the biology of plants. The field of plant-biotic interactions has recently coalesced around an integrated model. Major classes of molecular players both from plants and their associated organisms have been revealed. These include cell surface and intracellular immune receptors of plants as well as apoplastic and host-cell-translocated (cytoplasmic) effectors of the invading organism. This article focuses on effectors, molecules secreted by plant-associated organisms that alter plant processes. Effectors have emerged as a central class of molecules in our integrated view of plant-microbe interactions. Their study has significantly contributed to advancing our knowledge of plant hormones, plant development, plant receptors, and epigenetics. Many pathogen effectors are extraordinary examples of biological innovation; they include some of the most remarkable proteins known to function inside plant cells. Here, we review some of the key concepts that have emerged from the study of the effectors of plant-associated organisms. In particular, we focus on how effectors function in plant tissues and discuss future perspectives in the field of effector biology.

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“…This implies that InvE may transiently interact with the membrane or membrane-associated proteins of the SPI-1 T3SS (Kubori & Galán, 2002). Recently, Lara-Tejero et al (2011) reported that the secretion hierarchy between the translocases and effector proteins in the SPI-1 T3SS is established by a large complex that includes the SpaO-OrgA-OrgB sorting platform. It has also been determined that the T3SS-associated chaperones are responsible for the proper targeting of their cognate substrates to the sorting complex.…”

Section: Introductionmentioning

confidence: 99%

Molecular characterization of the InvE regulator in the secretion of type III secretion translocases in Salmonella enterica serovar Typhimurium

et al. 2013

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The type III secretion systems (T3SSs) are exploited by many Gram-negative pathogenic bacteria to deliver a set of effector proteins into the host cytosol during cell entry. The T3SS of Salmonella enterica serovar Typhimurium is composed of more than 20 proteins that constitute the membrane-associated base, the needle and the tip complex at the distal end of the T3SS needle. Membrane docking and piercing between the T3SS and host cells is followed by the secretion of effector proteins. Therefore, a secretion hierarchy among the substrates of the T3SS is required. The secretion of the pore-forming translocase proteins SipB, SipC and SipD is controlled by the T3SS regulator protein, InvE. During an attempt to identify the regions of InvE that are involved in T3SS regulation, it was observed that the secretion of SipB, SipC and SipD was inhibited when the C-terminal 52 amino acids were removed from InvE. In addition, InvE derivatives lacking the Nterminal 30 and 100 residues were unable to secrete translocases into the culture medium. Interestingly, in the absence of the N-terminal 180 residues of InvE, SipD is unstable, resulting in the hypersecretion of SipB. We also found that both the type III secretion signals of SipB and SptP were functionally interchangeable with the first 30 amino acids of InvE, which could allow the secretion of a reporter protein. These results indicate that InvE may have two functional domains responsible for regulating the secretion of translocases: an N-terminal secretion signal and a Cterminal regulatory domain.

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A Sorting Platform Determines the Order of Protein Secretion in Bacterial Type III Systems

Cited by 241 publications

References 35 publications

The inner rod protein controls substrate switching and needle length in a Salmonella type III secretion system

The inner rod protein controls substrate switching and needle length in a Salmonella type III secretion system

Effector Biology of Plant-Associated Organisms: Concepts and Perspectives

Molecular characterization of the InvE regulator in the secretion of type III secretion translocases in Salmonella enterica serovar Typhimurium

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