scholarly journals Functional characterization of the Erwinia chrysanthemi Outs protein, an element of a type II secretion system

Microbiology ◽  
1998 ◽  
Vol 144 (11) ◽  
pp. 3219-3228 ◽  
Author(s):  
V. E. Shevchik ◽  
G. Condemine
Keyword(s):  
Functional Characterization ◽  
Secretion System ◽  
Erwinia Chrysanthemi ◽  
Type Ii Secretion ◽  
Type Ii ◽  
Type Ii Secretion System

scholarly journals Functional Characterization of EpsC, a Component of the Type II Secretion System, in the Pathogenicity of Vibrio vulnificus

2011 ◽  
Vol 79 (10) ◽  
pp. 4068-4080 ◽  
Author(s):  
Won Hwang ◽  
Na Yeon Lee ◽  
Juri Kim ◽  
Mi-Ae Lee ◽  
Kun-Soo Kim ◽  
...  
Keyword(s):  
Vibrio Vulnificus ◽  
Outer Membrane Proteins ◽  
Functional Characterization ◽  
Secretion System ◽  
Host Cells ◽  
Type Ii Secretion ◽  
Type Ii ◽  
Content Type ◽  
Type Ii Secretion System ◽  
Secreted Factors

ABSTRACTEpsC, one of the components comprising the type II secretion system (T2SS), was isolated from a human-pathogenic bacterium,Vibrio vulnificus, to evaluate its role in eliciting virulence. AnespC-deleted mutant ofV. vulnificusdisplayed a reduced cytotoxicity to the human cell line HEp-2 and an attenuated virulence in a mouse model. This mutant exhibited dramatic defects in the secretion of diverse extracellular proteins, such as outer membrane proteins, transporters, and the known secreted factors, notably, a hemolysin (VvhA) and an elastase (VvpE). A defect in its secretion of proteins was restored by intranscomplementation of the intactepsCgene. Analyses of cellular fractions revealed that VvhA and VvpE of theΔepsCmutant were not excreted outside the cell but were present mainly in the periplasmic space. Examination of aV. vulnificusmutant deficient in TolC, a component of the T1SS, showed that it is not involved in the secretion of VvhA and VvpE but that it is necessary for the secretion of another major toxin ofV. vulnificus, RtxA. Therefore, the T2SS is required forV. vulnificuspathogenicity, which is mediated by at least two secreted factors, VvhA and VvpE, via facilitating the secretion and exposure of these factors to host cells.

scholarly journals Solution Structure of Homology Region (HR) Domain of Type II Secretion System

2012 ◽  
Vol 287 (12) ◽  
pp. 9072-9080 ◽  
Author(s):  
Shuang Gu ◽  
Geoff Kelly ◽  
Xiaohui Wang ◽  
Tom Frenkiel ◽  
Vladimir E. Shevchik ◽  
...  
Keyword(s):  
Solution Structure ◽  
Secretion System ◽  
Type Ii Secretion ◽  
Type Ii ◽  
Homology Region ◽  
Type Ii Secretion System

scholarly journals Generation of Xylose-inducible promoter tools for Pseudomonas species and their use in implicating a role for the Type II secretion system protein XcpQ in inhibition of corneal epithelial wound closure

2020 ◽  
Author(s):  
Jake D. Callaghan ◽  
Nicholas A. Stella ◽  
Kara M. Lehner ◽  
Benjamin R. Treat ◽  
Kimberly M. Brothers ◽  
...  
Keyword(s):  
Gene Expression ◽  
Wound Closure ◽  
Inducible Promoter ◽  
Secretion System ◽  
Type Ii Secretion ◽  
Type Ii ◽  
Corneal Epithelial ◽  
E Coli ◽  
Type Ii Secretion System ◽  
Promoter System

ABSTRACTTunable control of gene expression is an invaluable tool for biological experiments. In this study, we describe a new xylose-inducible promoter system and evaluate it in both Pseudomonas aeruginosa and P. fluorescens. The Pxut promoter derived from the P. flurorescens xut operon was incorporated into a broad host-range pBBR1-based plasmid and compared to the Escherichia coli-derived PBAD promoter using gfp as a reporter. GFP-fluorescence from the Pxut promoter was inducible in both Pseudomonas species, but not in E. coli, which may facilitate cloning of toxic genes using E. coli to generate plasmids. The Pxut promoter was expressed at a lower inducer concentration than PBAD in P. fluorescens and higher gfp levels were achieved using Pxut. Flow cytometry analysis indicated that Pxut was more leaky than PBAD in the tested Pseudomonas species, but was expressed in a higher proportion of cells when induced. D-xylose did not support growth of P. aeruginosa or P. fluorescens as a sole carbon source and is less expensive than many other commonly used inducers which could facilitate large scale applications. The efficacy of this system aided in demonstrating a role for the P. aeruginosa type II secretion system gene from xcpQ in bacterial inhibition of corneal epithelial cell wound closure. This study introduces a new inducible promoter system for gene expression for use in Pseudomonas species.ImportancePseudomonas species are enormously important in human infections, biotechnology, and as a model system for interrogating basic science questions. In this study we have developed a xylose-inducible promoter system and evaluated it in P. aeruginosa and P. fluorescens and found it to be suitable for the strong induction of gene expression. Furthermore, we have demonstrated its efficacy in controlled gene expression to show that a type 2 secretion system protein from P. aeruginosa, XcpQ, is important for host-pathogen interactions in a corneal wound closure model.

scholarly journals Structural and Functional Studies on the Interaction of GspC and GspD in the Type II Secretion System

2011 ◽  
Vol 7 (9) ◽  
pp. e1002228 ◽  
Author(s):  
Konstantin V. Korotkov ◽  
Tanya L. Johnson ◽  
Michael G. Jobling ◽  
Jonathan Pruneda ◽  
Els Pardon ◽  
...  
Keyword(s):  
Secretion System ◽  
Type Ii Secretion ◽  
Type Ii ◽  
Functional Studies ◽  
Type Ii Secretion System

scholarly journals Direct Involvement of Type II Secretion System in Extracellular Translocation of Shewanella oneidensis Outer Membrane Cytochromes MtrC and OmcA

2008 ◽  
Vol 190 (15) ◽  
pp. 5512-5516 ◽  
Author(s):  
Liang Shi ◽  
Shuang Deng ◽  
Matthew J. Marshall ◽  
Zheming Wang ◽  
David W. Kennedy ◽  
...  
Keyword(s):  
Cell Surface ◽  
Shewanella Oneidensis ◽  
Secretion System ◽  
Proteinase K ◽  
Type Ii Secretion ◽  
Type Ii ◽  
Direct Involvement ◽  
Type Ii Secretion System ◽  
Extracellular Release ◽  
Proteinase K Treatment

ABSTRACT MtrC and OmcA are cell surface-exposed lipoproteins important for reducing solid metal oxides. Deletions of type II secretion system (T2SS) genes reduced their extracellular release and their accessibility to the proteinase K treatment, demonstrating the direct involvement of T2SS in translocation of MtrC and OmcA to the bacterial cell surface.

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