Structure-Function Analysis of the Periplasmic &lt;b&gt;&lt;i&gt;Escherichia coli&lt;/i&gt;&lt;/b&gt; Cyclophilin PpiA in Relation to Biofilm Formation

Skagia, Aggeliki; Vezyri, Eleni; Grados, Konstantinos; Venieraki, Anastasia; Karpusas, Michael; Katinakis, Panagiotis; Dimou, Maria

doi:10.1159/000478858

Cited by 4 publications

(4 citation statements)

References 46 publications

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“…In Gram-negative bacteria the periplasmic cyclophilins appear to play a lesser role in virulence compared to their cytoplasmic counterparts. In L. pneumophila and Acinetobacter baylyi deletion of their periplasmic cyclophilins, Lpg1962 and rotA , respectively, resulted in no phenotype under the tested conditions. , In E. coli deletion of the ppiA gene results in increased swimming motility and biofilm production; the latter was independent of its PPIase activity . Meanwhile, in Brucella abortus , the causative agent of brucellosis, both cyclophilins CypA (PpiA) and CypB (PpiB) were essential for virulence with increased susceptibility to cellular stresses and decreased ability to cause chronic infection in hamsters shown.…”

Section: Cyclophilins In Bacteriamentioning

confidence: 99%

“…109,115 In E. coli deletion of the ppiA gene results in increased swimming motility and biofilm production; the latter was independent of its PPIase activity. 111 Meanwhile, in Brucella abortus, the causative agent of brucellosis, both cyclophilins CypA (PpiA) and CypB (PpiB) were essential for virulence with increased susceptibility to cellular stresses and decreased ability to cause chronic infection in hamsters shown. The reduction in virulence was restored when complementation studies were done with either cyclophilin indicating cyclophilins from B. abortus play a similar, interchangeable role.…”

Section: ■ Cyclophilins In Bacteriamentioning

confidence: 99%

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Targeting Protein Folding: A Novel Approach for the Treatment of Pathogenic Bacteria

et al. 2020

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Infectious diseases are a major cause of morbidity and mortality worldwide, exacerbated by increasing antibiotic resistance in many bacterial species. The development of drugs with new modes of action is essential. A leading strategy is antivirulence, with the aim to target bacterial proteins that are important in disease causation and progression but do not affect growth, resulting in reduced selective pressure for resistance. Immunophilins, a superfamily of peptidyl-prolyl cis–trans isomerase (PPIase) enzymes have been shown to be important for virulence in a broad-spectrum of pathogenic bacteria. This Perspective will provide an overview of the recent advances made in understanding the role of each immunophilin family, cyclophilins, FK506 binding proteins (FKBPs), and parvulins in bacteria. Inhibitor design and medicinal chemistry strategies for development of novel drugs against bacterial FKBPs will be discussed. Furthermore, drugs against human cyclophilins and parvulins will be reviewed in their current indication as antiviral and anticancer therapies.

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Section: Cyclophilins In Bacteriamentioning

confidence: 99%

Section: ■ Cyclophilins In Bacteriamentioning

confidence: 99%

Targeting Protein Folding: A Novel Approach for the Treatment of Pathogenic Bacteria

et al. 2020

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“…However, this involvement of PpiB in the biofilm formation phenotype does not involve its prolyl isomerase activity [32]. Biofilm formation was explored for FklB in order to elucidate the role of its PPIase function in this multicellular behavior, but also to investigate into its relation to swarming.…”

Section: Fklb Is Suppressing E Coli's Biofilm Formation Abilitymentioning

confidence: 99%

FK506-binding protein FklB is involved in biofilm formation through its peptidyl-prolyl isomerase activity

Zografou

Dimou

Katinakis

2020

Preprint

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FklB is a member of the FK506-binding proteins (FKBPs), a family that consists of five genes in Escherichia coli. Little is known about the physiological and functional role of FklB in bacterial movement. In the present study, FklB knock-out mutant ΔfklB presented an increased swarming and swimming motility and biofilm formation phenotype, suggesting that FklB is a negative regulator of these cellular processes.Complementation with Peptidyl-prolyl isomerase (PPIase)-deficient fklB gene (Y181A) revealed that the defects in biofilm formation were not restored by Y181A, indicating that PPIase activity of FklB is modulating biofilm formation in E. coli. The mean cell length of ΔfklB swarming cells was significantly smaller as compared to the wild-type BW25113. Furthermore, the mean cell length of swarming and swimming wild-type and ΔfklB cells overexpressing fklB or Y181A was considerably larger, suggesting that PPIase activity of FklB plays a role in cell elongation and/or cell division. A multi-copy suppression assay demonstrated that defects in motility and biofilm phenotype were compensated by overexpressing sets of PPIase-encoding genes. Taken together, our data represent the first report demonstrating the involvement of FklB in cellular functions of E. coli.

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“…Other protein like SurA from E. coli, Shigella exneri, and Salmonella Typhimurium also help to cell adhesion and invasion of (Sydenham et al 2000). In E. coli, PpiB also controls cell division by modulating the function of various proteins which are directly or indirectly associated with the cell division (Skagia et al 2017). In this study, the role of Peptidyl-prolyl cis-trans isomerase-A type of cyclosporin is explored.…”

Section: Introductionmentioning

confidence: 99%

Purification and characterization of Cyclophilin: a protein associated with protein folding in Salmonella Typhimurium

Kumawat

Chaudhary²,

Nabi

et al. 2021

Arch Microbiol

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Salmonella Typhimurium (ST) is the zoonotic pathogenic Gram-negative bacteria to causes infectious disease in humans as well as in animals. It causes gastrointestinal illness and fever called salmonellosis, which is foodborne diarrheal and leading cause of millions of deaths worldwide. Salmonella enterica serovar Typhimurium (S. Typhimurium) during its pathogenesis takeaway the actin cytoskeleton of their host cells and this is the crucial step of its infection cycle. Cyclophilin A, a type of peptidyl-prolyl isomerase that's encoded by the ppiA gene in ST, plays pleiotropic roles in maintaining bacterial physiology. In this research, the proteomic characterization of the peptidyl-prolyl cis-trans isomerase-A (Cyclophilin A) from Salmonella Typhimurium is reported. Cyclophilin A (CypA) protein from Salmonella Typhimurium proved to be a highly conserved protein sequence and highly homologous compared to other organisms. This protein was expressed in Escherichia coli and then puri ed in a recombinant form protein exhibited a characteristic PPIases activity (V max = 0.8752 ± 0.13892 µmoles/ min, K m = 0.9315 ± 0.5670 µM) in comparison to control. Also, in this study the mass spectrometry analysis of Cyp A proteinpeptide showed the highest sequence similarity with the cyclophilin protein of Salmonella. PPIases proteins enzyme data suggest that Ppi-A has roles in the protein folding that may be contributing to the virulence of Salmonella by isomerization of protein outline. These results suggest an active and vital role of this protein in protein folding along with regulation in Salmonella Typhimurium.

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Structure-Function Analysis of the Periplasmic <b><i>Escherichia coli</i></b> Cyclophilin PpiA in Relation to Biofilm Formation

Cited by 4 publications

References 46 publications

Targeting Protein Folding: A Novel Approach for the Treatment of Pathogenic Bacteria

Targeting Protein Folding: A Novel Approach for the Treatment of Pathogenic Bacteria

FK506-binding protein FklB is involved in biofilm formation through its peptidyl-prolyl isomerase activity

Purification and characterization of Cyclophilin: a protein associated with protein folding in Salmonella Typhimurium

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