The ability of haemolysins expressed by atypical enteropathogenic Escherichia coli to bind to extracellular matrix components

Magalhães, Caroline Arantes; Rossato, Sarita S.; Barbosa, Angela Silva; Santos, Thiago O. dos; Elias, Waldir P.; Sircili, Marcelo Palma; Piazza, Roxane M. F.

doi:10.1590/s0074-02762011000200005

Cited by 10 publications

(10 citation statements)

References 46 publications

(39 reference statements)

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“…The high adhesiveness ability of the O26:H11 strain to ECM components, mainly fibronectin and laminin [ 7 ], prompted us to characterize in vitro binding ability of BA2103 to fibronectin with the aim of characterizing putative bacterial proteins involved in this interaction. Our results confirmed the binding of BA2103 bacterial cells to fibronectin.…”

Section: Discussionmentioning

confidence: 99%

“…Molecular typing of fliC defined the H type of 2271-1/85 strain as H11 [ 39 ]. Binding ability to ECM of supernatant proteins from BA2103 was described elsewhere [ 7 ]. A non-pathogenic K12 E. coli DH5α was included as a control strain [ 40 ].…”

Section: Methodsmentioning

confidence: 99%

“…Moreover, EPEC is distinguished by the presence of EPEC adherence factor plasmid (pEAF) in typical EPEC (tEPEC) and its absence in atypical EPEC (aEPEC) [ 4 ]. Also, lack of bundle-forming pilus (BFP) production [ 5 , 6 ], presence of hemolysins [ 7 ] and autotransporter proteins [ 8 , 9 ] existing in other diarrheagenic E. coli pathotypes characterize aEPEC [ 10 , 11 ]. In tEPEC, the role of BFP either in initial contact or in bacteria-bacteria interaction is well established [ 12 , 13 ].…”

Section: Introductionmentioning

confidence: 99%

“…Previous results from our group demonstrated that a subset of atypical EPEC presented ability to bind to immobilized ECM proteins. Among them, the O26:H11 (BA2103) strain consistently presented the highest binding ability to cellular fibronectin [ 7 ]. Taking these results in consideration, we investigated in the current study putative candidates of this particular strain that might mediate binding to cellular fibronectin.…”

Section: Introductionmentioning

confidence: 99%

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Flagellin and GroEL mediates in vitro binding of an atypical enteropathogenic Escherichia coli to cellular fibronectin

et al. 2015

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BackgroundEnteropathogenic Escherichia coli (EPEC) is distinguished mainly by the presence of EPEC adherence factor plasmid (pEAF) in typical EPEC (tEPEC) and its absence in atypical EPEC (aEPEC). The initial adherence to the intestinal mucosa is complex and mediated by adhesins other than bundle-forming pilus, which is not produced by aEPEC. Extracellular matrix (ECM) proteins of eukaryotic cells are commonly recognized by bacterial adhesins. Therefore, binding to ECM proteins may facilitate colonization, invasion and/or signaling by intestinal pathogens. Previous studies from our group demonstrated that aEPEC O26:H11 (strain BA2103) showed high binding activity to fibronectin, not shared by its counterpart, aEPEC O26:HNM.ResultsIn the present study, using mass spectrometry after fibronectin-associated immunoprecipitation, two proteins, flagellin (50 kDa) and GroEL (52 kDa), were identified and BA2103 binding ability to fibronectin was inhibited in the presence of anti-H11 and anti-GroEL sera, but not by either naïve rabbit or other unrelated sera. It was also observed that the presence of purified flagellin inhibits adhesion of BA2103 to cellular fibronectin in a dose-dependent manner. Additionally, BA2103 GroEL is similar to the same protein of uropathogenic E. coli.ConclusionsOur results suggest that flagellin may play a role in the in vitro interaction of BA2103 with cellular fibronectin, and GroEL can be an accessory protein in this process.Electronic supplementary materialThe online version of this article (doi:10.1186/s12866-015-0612-4) contains supplementary material, which is available to authorized users.

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Section: Discussionmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Flagellin and GroEL mediates in vitro binding of an atypical enteropathogenic Escherichia coli to cellular fibronectin

et al. 2015

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“…Indeed, purified PLCH causes vascular permeability, end organ damage, and death when injected into mice in high doses (Meyers et al, 1992 andWargo et al, 2011). These hemolytic enzymes are cytolytic toxic proteins produced by wide range of bacteria causing lyses of erythrocytes, disrupting the function of the plasma membrane (Magalhaes et al, 2011).…”

Section: Abstract: Pseudomonas Aeruginosa; Phospholipase C Antigenicmentioning

confidence: 99%

Characterization and Immunological Properties of Pseudomonas aeruginosa Hemolytic Phospholipase C

2014

Egypt. J. Bot.

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Characterization of the universal stress protein F from atypical enteropathogenic Escherichia coli and its prevalence in Enterobacteriaceae

et al. 2016

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Atypical enteropathogenic Escherichia coli (aEPEC) are heterogeneous strains in terms of serotypes, adherence patterns and the presence of novel virulence factors. This heterogeneity is intriguing, promoting studies trying to characterize these novel proteins and to better comprehend this pathotype group. In a previous study analyzing low‐molecular mass proteomes of four representative aEPEC strains of three different adhesion phenotypes, we classified proteins according to their annotated function, with most of them being involved in metabolism and transport; while some of them were classified as hypothetical proteins. The majority of the hypothetical proteins were homologue products of genes identified in the genome of enterohemorrhagic E. coli. One of the hypothetical proteins was annotated as Z2335, with orthologue in EPEC, and by bioinformatics analysis, this protein was revealed to be the universal stress protein F (UspF). Thus, herein we successfully obtained a recombinant UspF protein from aEPEC, which is a α/β, ATP‐binding protein involved in stress response, with comparable protein production among the four studied strains, but showing noteworthy differences when cultivated in different stress conditions, also present in other enterobacterial species, such as Shigella sonnei and Citrobacter freundii. Furthermore, our results confirm that the Usp protein superfamily encompasses a conserved group of proteins involved in stress resistance in aEPEC and other Enterobacteriaceae.

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The ability of haemolysins expressed by atypical enteropathogenic Escherichia coli to bind to extracellular matrix components

Abstract: Typical and atypical enteropathogenic

Cited by 10 publications

References 46 publications

Flagellin and GroEL mediates in vitro binding of an atypical enteropathogenic Escherichia coli to cellular fibronectin

Flagellin and GroEL mediates in vitro binding of an atypical enteropathogenic Escherichia coli to cellular fibronectin

Characterization and Immunological Properties of Pseudomonas aeruginosa Hemolytic Phospholipase C

Characterization of the universal stress protein F from atypical enteropathogenic Escherichia coli and its prevalence in Enterobacteriaceae

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