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Open AccessJournal ArticleDOI

Protein Export According to Schedule: Architecture, Assembly, and Regulation of Type III Secretion Systems from Plant- and Animal-Pathogenic Bacteria

TLDR
The aim of this review is to summarize the current knowledge of T3S system components and associated control proteins from both plant- and animal-pathogenic bacteria.
Abstract
Flagellar and translocation-associated type III secretion (T3S) systems are present in most gram-negative plant- and animal-pathogenic bacteria and are often essential for bacterial motility or pathogenicity. The architectures of the complex membrane-spanning secretion apparatuses of both systems are similar, but they are associated with different extracellular appendages, including the flagellar hook and filament or the needle/pilus structures of translocation-associated T3S systems. The needle/pilus is connected to a bacterial translocon that is inserted into the host plasma membrane and mediates the transkingdom transport of bacterial effector proteins into eukaryotic cells. During the last 3 to 5 years, significant progress has been made in the characterization of membrane-associated core components and extracellular structures of T3S systems. Furthermore, transcriptional and posttranscriptional regulators that control T3S gene expression and substrate specificity have been described. Given the architecture of the T3S system, it is assumed that extracellular components of the secretion apparatus are secreted prior to effector proteins, suggesting that there is a hierarchy in T3S. The aim of this review is to summarize our current knowledge of T3S system components and associated control proteins from both plant- and animal-pathogenic bacteria.

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Journal ArticleDOI

Secretion systems in Gram-negative bacteria: structural and mechanistic insights

TL;DR: The structural and mechanistic relationships between these single- and double-membrane-embedded systems are explored, and how this knowledge can be exploited for the development of new antimicrobial strategies are discussed.
Journal ArticleDOI

Bacterial Secretion Systems – An overview

TL;DR: This chapter reviews the canonical features of several common bacterial protein secretion systems, as well as their roles in promoting the virulence of bacterial pathogens, and addresses recent findings that indicate that the innate immune system of the host can detect and respond to the presence ofprotein secretion systems during mammalian infection.
Journal ArticleDOI

Bacterial type III secretion systems: specialized nanomachines for protein delivery into target cells

TL;DR: One of the most exciting developments in the field of bacterial pathogenesis in recent years is the discovery that many pathogens utilize complex nanomachines to deliver bacterially encoded effector proteins into target eukaryotic cells.
Journal ArticleDOI

The Role of the Bacterial Flagellum in Adhesion and Virulence

TL;DR: The latest or most important findings regarding flagellar adhesive and invasive properties are examined, especially focusing on the flageLLum as a potential virulence factor.
Journal ArticleDOI

Assembly, structure, function and regulation of type III secretion systems

TL;DR: Current knowledge of the structure and function of T3SSs is summarized, which should aid mechanism-based drug design and facilitate their manipulation for biotechnological applications.
References
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Journal ArticleDOI

Nod1 Detects a Unique Muropeptide from Gram-Negative Bacterial Peptidoglycan

TL;DR: It is shown that human Nod1 specifically detects a unique diaminopimelate-containing N-acetylglucosamine–N-acetelmuramic acid tripeptide motif found in Gram-negative bacterial peptidoglycan, resulting in activation of the transcription factor NF-κB pathway.
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Cytoplasmic flagellin activates caspase-1 and secretion of interleukin 1β via Ipaf

TL;DR: It is shown here that cytosolic bacterial flagellin activated caspase-1 through Ipaf but was independent of Toll-like receptor 5, a known flageLLin sensor, which raises the possibility that the salmonella pathogenicity island 1 type III secretion system cannot completely exclude 'promiscuous' secretion of flagella.
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The NLRC4 inflammasome receptors for bacterial flagellin and type III secretion apparatus

TL;DR: It is shown that NAIP5, a BIR-domain NLR protein required for Legionella pneumophila replication in mouse macrophages, is a universal component of the flagellin–NLRC4 pathway and predicts that the remaining NAIP family members may recognize other unidentified microbial products to activate NLRC4 inflammasome-mediated innate immunity.
Journal ArticleDOI

Supramolecular structure of the Salmonella typhimurium type III protein secretion system.

TL;DR: Electron microscopy revealed supramolecular structures spanning the inner and outer membranes of flagellated and nonflagllated strains; such structures were not detected in strains carrying null mutations in components of the type III apparatus.
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