The Xanthomonas oryzae pv. oryzae type IV pilus alignment subcomplex protein PilN contributes to regulation of bacterial surface‐associated behaviours and T3SS system

2020 ◽  
Vol 69 (4) ◽  
pp. 744-755
Author(s):  
Yilang Li ◽  
Yichao Yan ◽  
Songge Deng ◽  
Cuiping Zhang ◽  
Fazal Haq ◽  
...  
Keyword(s):  
Xanthomonas Oryzae ◽  
Type Iv Pilus ◽  
Bacterial Surface ◽  
Type Iv

scholarly journals Obstruction of pilus retraction stimulates bacterial surface sensing

2017 ◽  
Author(s):  
Courtney K. Ellison ◽  
Jingbo Kan ◽  
Rebecca S. Dillard ◽  
David T. Kysela ◽  
Cheri M. Hampton ◽  
...  
Keyword(s):  
Genetic Modification ◽  
Caulobacter Crescentus ◽  
Physiological Changes ◽  
Type Iv Pilus ◽  
Dynamic Nature ◽  
Surface Attachment ◽  
Bacterial Surface ◽  
Type Iv ◽  
Surface Sensing ◽  
Surface Contact

AbstractSurface association provides numerous fitness advantages to bacteria. Thus, it is critical for bacteria to recognize surface contact and to consequently initiate physiological changes required for a surface-associated lifestyle (1). Ubiquitous microbial appendages called pili are involved in sensing surfaces and mediating downstream surface-associated behaviors (2–6). The mechanism by which pili mediate surface sensing remains unknown, largely due to the difficulty to visualize their dynamic nature and to directly modulate their activity without genetic modification. Here, we show thatCaulobacter crescentuspili undergo dynamic cycles of extension and retraction that cease within seconds of surface contact, and this arrest of pilus activity coincides with surface-stimulated holdfast synthesis. By physically blocking pili, we show that imposing resistance to pilus retraction is sufficient to stimulate holdfast synthesis in the absence of surface contact. Thus, resistance to type IV pilus retraction upon surface attachment is used for surface sensing.One Sentence SummaryBacteria use the tension imparted on retracting pilus fibers upon their binding to a surface for surface sensing.

scholarly journals Yersinia pseudotuberculosis Harbors a Type IV Pilus Gene Cluster That Contributes to Pathogenicity

2002 ◽  
Vol 70 (11) ◽  
pp. 6196-6205 ◽  
Author(s):  
François Collyn ◽  
Marie-Annick Léty ◽  
Shamila Nair ◽  
Vincent Escuyer ◽  
Amena Ben Younes ◽  
...  
Keyword(s):  
Gene Cluster ◽  
Yersinia Pseudotuberculosis ◽  
Open Reading Frames ◽  
Host Cells ◽  
Gram Negative Bacteria ◽  
Type Iv Pilus ◽  
Chromosomal Locus ◽  
Bacterial Surface ◽  
Type Iv ◽  
Reading Frames

ABSTRACT Fimbriae have been shown to play an essential role in the adhesion of pathogenic gram-negative bacteria to host cells. In the enteroinvasive bacterium Yersinia pseudotuberculosis, we characterized a previously unknown 11-kb chromosomal locus involved in the synthesis of type IV pili. The locus consists of 11 open reading frames forming a polycistronic unit and encoding putative Pil proteins, PilLMNOPQRSUVW. When introduced into Escherichia coli, the Y. pseudotuberculosis operon reconstituted bundles of filaments at a pole on the bacterial surface, demonstrating that the pil locus was functional in a heterogenous genetic background. Environmental factors regulated transcription of the Y. pseudotuberculosis operon; in particular, temperature, osmolarity, and oxygen tension were critical cues. Deletion of the type IV pilus gene cluster was associated with a reduction of Y. pseudotuberculosis pathogenicity for mice infected orally. Forty-one percent of Y. pseudotuberculosis strains isolated from human or animal sources harbored the type IV pilus locus. Therefore, the pil locus of Y. pseudotuberculosis might constitute an “adaptation island,” permitting the microorganism to colonize a vast reservoir.

scholarly journals Inhibitors of theNeisseria meningitidisPilF ATPase provoke type IV pilus disassembly

2019 ◽  
Vol 116 (17) ◽  
pp. 8481-8486 ◽  
Author(s):  
Flore Aubey ◽  
Jean-Philippe Corre ◽  
Youxin Kong ◽  
Ximing Xu ◽  
Dorian Obino ◽  
...  
Keyword(s):  
Bacterial Adhesion ◽  
Therapeutic Option ◽  
Host Cells ◽  
Type Iv Pilus ◽  
Meningococcal Infections ◽  
Bacterial Surface ◽  
Type Iv ◽  
Pilus Biogenesis ◽  
Attractive Therapeutic Target ◽  
Relationship Of

Despite the availability of antibiotics and vaccines,Neisseria meningitidisremains a major cause of meningitis and sepsis in humans. Due to its extracellular lifestyle, bacterial adhesion to host cells constitutes an attractive therapeutic target. Here, we present a high-throughput microscopy-based approach that allowed the identification of compounds able to decrease type IV pilus-mediated interaction of bacteria with endothelial cells in the absence of bacterial or host cell toxicity. Compounds specifically inhibit the PilF ATPase enzymatic activity that powers type IV pilus extension but remain inefficient on the ATPase that promotes pilus retraction, thus leading to rapid pilus disappearance from the bacterial surface and loss of pili-mediated functions. Structure activity relationship of the most active compound identifies specific moieties required for the activity of this compound and highlights its specificity. This study therefore provides compounds targeting pilus biogenesis, thereby inhibiting bacterial adhesion, and paves the way for a novel therapeutic option for meningococcal infections.

scholarly journals Type IV Pilus Assembly Proficiency and Dynamics Influence Pilin Subunit Phospho-Form Macro- and Microheterogeneity in Neisseria gonorrhoeae

PLoS ONE ◽  
2014 ◽  
Vol 9 (5) ◽  
pp. e96419 ◽  
Author(s):  
Åshild Vik ◽  
Jan Haug Anonsen ◽  
Finn Erik Aas ◽  
Finn Terje Hegge ◽  
Norbert Roos ◽  
...  
Keyword(s):  
Neisseria Gonorrhoeae ◽  
Type Iv Pilus ◽  
Type Iv ◽  
Pilin Subunit ◽  
Pilus Assembly

Identification and initial characterization of a new pair of sibling sRNAs of Neisseria gonorrhoeae involved in type IV pilus biogenesis

Microbiology ◽  
2021 ◽  
Vol 167 (9) ◽  
Author(s):  
Marie Zachary ◽  
Susanne Bauer ◽  
Maximilian Klepsch ◽  
Katharina Wagler ◽  
Bruno Hüttel ◽  
...  
Keyword(s):  
Target Genes ◽  
Target Prediction ◽  
Type Iv Pilus ◽  
Content Type ◽  
Type Iv ◽  
Gene Expression Control ◽  
Initial Characterization ◽  
Pilus Biogenesis ◽  
Regulatory Rnas

Non-coding regulatory RNAs mediate post-transcriptional gene expression control by a variety of mechanisms relying mostly on base-pairing interactions with a target mRNA. Though a plethora of putative non-coding regulatory RNAs have been identified by global transcriptome analysis, knowledge about riboregulation in the pathogenic Neisseriae is still limited. Here we report the initial characterization of a pair of sRNAs of N. gonorrhoeae , TfpR1 and TfpR2, which exhibit a similar secondary structure and identical single-stranded seed regions, and therefore might be considered as sibling sRNAs. By combination of in silico target prediction and sRNA pulse expression followed by differential RNA sequencing we identified target genes of TfpR1 which are involved in type IV pilus biogenesis and DNA damage repair. We provide evidence that members of the TfpR1 regulon can also be targeted by the sibling TfpR2.

scholarly journals Purification and Three-Dimensional Electron Microscopy Structure of the Neisseria meningitidis Type IV Pilus Biogenesis Protein PilG

2007 ◽  
Vol 189 (17) ◽  
pp. 6389-6396 ◽  
Author(s):  
Richard F. Collins ◽  
Muhammad Saleem ◽  
Jeremy P. Derrick
Keyword(s):  
Electron Microscopy ◽  
Neisseria Meningitidis ◽  
Metal Ion ◽  
Polyacrylamide Gel Electrophoresis ◽  
Three Dimensional ◽  
Type Ii Secretion ◽  
Type Ii ◽  
Type Iv Pilus ◽  
Type Iv ◽  
Pilus Biogenesis

ABSTRACT Type IV pili are surface-exposed retractable fibers which play a key role in the pathogenesis of Neisseria meningitidis and other gram-negative pathogens. PilG is an integral inner membrane protein and a component of the type IV pilus biogenesis system. It is related by sequence to the extensive GspF family of secretory proteins, which are involved in type II secretion processes. PilG was overexpressed and purified from Escherichia coli membranes by detergent extraction and metal ion affinity chromatography. Analysis of the purified protein by perfluoro-octanoic acid polyacrylamide gel electrophoresis showed that PilG formed dimers and tetramers. A three-dimensional (3-D) electron microscopy structure of the PilG multimer was determined using single-particle averaging applied to samples visualized by negative staining. Symmetry analysis of the unsymmetrized 3-D volume provided further evidence that the PilG multimer is a tetramer. The reconstruction also revealed an asymmetric bilobed structure approximately 125 Å in length and 80 Å in width. The larger lobe within the structure was identified as the N terminus by location of Ni-nitrilotriacetic acid nanogold particles to the N-terminal polyhistidine tag. We propose that the smaller lobe corresponds to the periplasmic domain of the protein, with the narrower “waist” region being the transmembrane section. This constitutes the first report of a 3-D structure of a member of the GspF family and suggests a physical basis for the role of the protein in linking cytoplasmic and periplasmic protein components of the type II secretion and type IV pilus biogenesis systems.

scholarly journals Genomic and Gene-Expression Comparisons among Phage-Resistant Type-IV Pilus Mutants of Pseudomonas syringae pathovar phaseolicola

PLoS ONE ◽  
2015 ◽  
Vol 10 (12) ◽  
pp. e0144514 ◽  
Author(s):  
Mark Sistrom ◽  
Derek Park ◽  
Heath E. O’Brien ◽  
Zheng Wang ◽  
David S. Guttman ◽  
...  
Keyword(s):  
Gene Expression ◽  
Pseudomonas Syringae ◽  
Type Iv Pilus ◽  
Type Iv
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