The FliK protein and flagellar hook‐length control

Waters, Richard C.; O’Toole, Paul W.; Ryan, Kevin

doi:10.1110/ps.072785407

Cited by 55 publications

(50 citation statements)

References 99 publications

(134 reference statements)

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“…The extremely limited number of exclusive SNPs in food and human isolates within the outbreak is an additional compelling element indicative of the fact that these two groups of isolates did not have enough evolutionary time to significantly differentiate, indicating they belong to the same clone. A BLAST analysis of these SNPs against the Virulence Factors Database revealed three genes of particular interest: (i) fliK, coding for a flagellar hook-length control protein (41), (ii) sthD, a gene coding for a fimbrial outer membrane usher protein (42), and (iii) rfbD, coding for a UDP-galactopyranose mutase precursor involved in the synthesis of the O antigen of the lipopolysaccharide (LPS). All three proteins are virulence determinants in Salmonella (43)(44)(45)(46).…”

Section: Discussionmentioning

confidence: 99%

Differential Single Nucleotide Polymorphism-Based Analysis of an Outbreak Caused by Salmonella enterica Serovar Manhattan Reveals Epidemiological Details Missed by Standard Pulsed-Field Gel Electrophoresis

et al. 2015

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We retrospectively analyzed a rare Salmonella enterica serovar Manhattan outbreak that occurred in Italy in 2009 to evaluate the potential of new genomic tools based on differential single nucleotide polymorphism (SNP) analysis in comparison with the gold standard genotyping method, pulsed-field gel electrophoresis. A total of 39 isolates were analyzed from patients (n ‫؍‬ 15) and food, feed, animal, and environmental sources (n ‫؍‬ 24), resulting in five different pulsed-field gel electrophoresis (PFGE) profiles. Isolates epidemiologically related to the outbreak clustered within the same pulsotype, SXB_BS.0003, without any further differentiation. Thirty-three isolates were considered for genomic analysis based on different sets of SNPs, core, synonymous, nonsynonymous, as well as SNPs in different codon positions, by Bayesian and maximum likelihood algorithms. Trees generated from core and nonsynonymous SNPs, as well as SNPs at the second and first plus second codon positions detailed four distinct groups of isolates within the outbreak pulsotype, discriminating outbreak-related isolates of human and food origins. Conversely, the trees derived from synonymous and third-codon-position SNPs clustered food and human isolates together, indicating that all outbreak-related isolates constituted a single clone, which was in line with the epidemiological evidence. Further experiments are in place to extend this approach within our regional enteropathogen surveillance system. Salmonellosis is a major food-borne disease worldwide, with an estimated 93.8 million cases occurring each year, resulting in 155,000 deaths (1). The European Union summary report on trends and sources of zoonoses, zoonotic agents and food-borne outbreaks (2) indicated that nontyphoid salmonellosis was the second most reported food-borne zoonosis in Europe in 2012, trailing only behind Campylobacter jejuni infection. The 2012 overall notification rate for human salmonellosis in the European Union (EU) was 22.2 episodes per 100,000 population, for a total of 91,034 confirmed cases, with hospitalization and mortality rates of 45.1% and 0.14%, respectively. The highest proportions of Salmonella-positive foodstuff samples were reported for fresh turkey, poultry, and pork at 4.4%, 4.1%, and 0.7%, respectively (2). In order to manage this food-borne infection and to limit its health and economic burdens, surveillance programs have developed and implemented DNA-based subtyping methods to identify outbreaks in a timely manner and to trace infections back to their food sources. Over the past decades, the two most intensively used protocols for Salmonella subtyping have been pulsed-field gel electrophoresis (PFGE) and multilocus variable-number tandemrepeat analysis (MLVA) (3). Unfortunately, these methods rely on just few features of the entire bacterial genome (rare restriction sites for PFGE or few polymorphic loci for MLVA) to assess the relatedness of different isolates. During epidemiological investigations of food-borne outbreaks, this limitation mi...

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Section: Discussionmentioning

confidence: 99%

Differential Single Nucleotide Polymorphism-Based Analysis of an Outbreak Caused by Salmonella enterica Serovar Manhattan Reveals Epidemiological Details Missed by Standard Pulsed-Field Gel Electrophoresis

et al. 2015

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“…A pause in secretion and/or a stretched conformation of the T3S4 protein presumably allows the interaction of the C-terminal domain with the C-terminal cytoplasmic domain of FlhB/YscU family members and thus signals the substrate specificity switch (19,25,72,73). It is unlikely, however, that the molecular ruler model is applicable to plant-pathogenic bacteria, because the extracellular pilus that is associated with the T3S systems of plant-pathogenic bacteria is too long to be "bridged" by a single proteinaceous ruler.…”

Section: Discussionmentioning

confidence: 99%

“…Given the architecture of translocation-associated and flagellar T3S systems, it is assumed that the assembly of extracellular components of the secretion apparatus precedes effector protein translocation, suggesting a hierarchical process (19,31,73). Components of the extracellular pilus are therefore presumably secreted prior to translocon and effector proteins, which implies that the substrate specificity of the T3S system switches from "early" to "late" substrates.…”

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confidence: 99%

Functional Characterization of the Type III Secretion Substrate Specificity Switch Protein HpaC from Xanthomonas campestris pv. vesicatoria

Schulz

Büttner

2011

Infect Immun

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Pathogenicity of Xanthomonas campestris pv. vesicatoria depends on a type III secretion (T3S) system which translocates effector proteins into eukaryotic cells and is associated with an extracellular pilus and a translocon in the host plasma membrane. T3S substrate specificity is controlled by the cytoplasmic switch protein HpaC, which interacts with the C-terminal domain of the inner membrane protein HrcU (HrcU C ). HpaC promotes the secretion of translocon and effector proteins but prevents the efficient secretion of the early T3S substrate HrpB2, which is required for pilus assembly. In this study, complementation assays with serial 10-amino-acid HpaC deletion derivatives revealed that the T3S substrate specificity switch depends on N-and C-terminal regions of HpaC, whereas amino acids 42 to 101 appear to be dispensable for the contribution of HpaC to the secretion of late substrates. However, deletions in the central region of HpaC affect the secretion of HrpB2, suggesting that the mechanisms underlying HpaC-dependent control of early and late substrates can be uncoupled. The results of interaction and expression studies with HpaC deletion derivatives showed that amino acids 112 to 212 of HpaC provide the binding site for HrcU C and severely reduce T3S when expressed ectopically in the wild-type strain. We identified a conserved phenylalanine residue at position 175 of HpaC that is required for both protein function and the binding of HpaC to HrcU C . Taking these findings together, we concluded that the interaction between HpaC and HrcU C is essential but not sufficient for T3S substrate specificity switching.Gram-negative plant-pathogenic bacteria of the genus Xanthomonas infect a large number of mono-and dicotyledonous plants and cause severe yield losses worldwide (43). In most cases, bacteria utilize a type III secretion (T3S) system to successfully conquer their respective host plants (12). T3S systems are essential pathogenicity factors of many Gram-negative plant-and animal-pathogenic bacteria and mediate the translocation of bacterial proteins, also referred to as type III effector proteins, into the cytosol of eukaryotic cells (12,31,60). Type III effector proteins presumably interfere with host cellular functions such as basal immune responses, to the benefit of the pathogen, and thus promote bacterial multiplication (5,12,36,69).In our laboratory, we study Xanthomonas campestris pv. vesicatoria, which is the causal agent of bacterial spot disease in pepper and tomato plants and one of the model systems for the analysis of bacterial pathogenicity factors (12). During natural infection, bacteria enter the plant tissue via openings on the plant surface, such as stomata, hydathodes, or wounds, and colonize the intercellular spaces. Bacterial multiplication depends on the T3S system, which injects approximately 30 effector proteins (Xops [Xanthomonas outer proteins]) into the plant cell and is encoded by the chromosomal hrp (hypersensitive response and pathogenicity) gene cluster (10, 69). The hrp gen...

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“…The aim of this review is to summarize our current knowledge of the architecture of T3S systems and the control mechanisms underlying T3S in plant-and animal-pathogenic bacteria. For a detailed description of individual proteins or regulatory mechanisms, the reader is also referred to excellent previous overview articles that provide summaries on the following topics: translocation-associated T3S systems (29,72,105,161,199,217,557), flagellar T3S systems (92,161,343,377,428,549), T3S chaperones (175,431), structures and functions of individual components of T3S systems (46,70,243,281,283,349,353,389,395,482), and control mechanisms underlying T3S and gene expression (64,106,129,212,370,421,547,555,588).…”

mentioning

confidence: 99%

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

Büttner

2012

Microbiol Mol Biol Rev

366

482

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SUMMARY 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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The FliK protein and flagellar hook‐length control

Cited by 55 publications

References 99 publications

Differential Single Nucleotide Polymorphism-Based Analysis of an Outbreak Caused by Salmonella enterica Serovar Manhattan Reveals Epidemiological Details Missed by Standard Pulsed-Field Gel Electrophoresis

Differential Single Nucleotide Polymorphism-Based Analysis of an Outbreak Caused by Salmonella enterica Serovar Manhattan Reveals Epidemiological Details Missed by Standard Pulsed-Field Gel Electrophoresis

Functional Characterization of the Type III Secretion Substrate Specificity Switch Protein HpaC from Xanthomonas campestris pv. vesicatoria

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

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