Expression of type I pili is abolished in verotoxin-producing<i>Escherichia coli</i>O157

Enami, Mika; Nakasone, Noboru; Honma, Yasuko; Kakinohana, Shige; Kudaka, Jun; Iwanaga, Masaaki

doi:10.1111/j.1574-6968.1999.tb08764.x

Cited by 25 publications

(2 citation statements)

References 16 publications

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“…It has been shown that strains of seropathotype A isolates are unable to express type 1 fimbriae due to a 16-bp deletion in the regulatory switch region of fimA (52)(53)(54). Interestingly, 7 seropathotype A isolates were able to agglutinate yeast in a mannose-independent manner and were able to autoagglutinate ( Fig.…”

Section: Discussionmentioning

confidence: 99%

Biofilm-Forming Abilities of Shiga Toxin-Producing Escherichia coli Isolates Associated with Human Infections

Vogeleer

Tremblay

Jubelin³

et al. 2016

Appl Environ Microbiol

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bForming biofilms may be a survival strategy of Shiga toxin-producing Escherichia coli to enable it to persist in the environment and the food industry. Here, we evaluate and characterize the biofilm-forming ability of 39 isolates of Shiga toxin-producing Escherichia coli isolates recovered from human infection and belonging to seropathotypes A, B, or C. The presence and/or production of biofilm factors such as curli, cellulose, autotransporter, and fimbriae were investigated. The polymeric matrix of these biofilms was analyzed by confocal microscopy and by enzymatic digestion. Cell viability and matrix integrity were examined after sanitizer treatments. Isolates of the seropathotype A (O157:H7 and O157:NM), which have the highest relative incidence of human infection, had a greater ability to form biofilms than isolates of seropathotype B or C. Seropathotype A isolates were unique in their ability to produce cellulose and poly-N-acetylglucosamine. The integrity of the biofilms was dependent on proteins. Two autotransporter genes, ehaB and espP, and two fimbrial genes, z1538 and lpf2, were identified as potential genetic determinants for biofilm formation. Interestingly, the ability of several isolates from seropathotype A to form biofilms was associated with their ability to agglutinate yeast in a mannose-independent manner. We consider this an unidentified biofilmassociated factor produced by those isolates. Treatment with sanitizers reduced the viability of Shiga toxin-producing Escherichia coli but did not completely remove the biofilm matrix. Overall, our data indicate that biofilm formation could contribute to the persistence of Shiga toxin-producing Escherichia coli and specifically seropathotype A isolates in the environment. Shiga toxin-producing Escherichia coli (STEC) strains, including enterohemorrhagic E. coli (EHEC), are food-borne and waterborne human enteric pathogens responsible for infections. They are associated with important public health concerns in developed countries. Symptoms associated with STEC infections range from abdominal cramps and bloody diarrhea to postinfectious complications, such as hemolytic-uremic syndrome (HUS). HUS, a life-threatening complication of STEC infections, is a consequence of Shiga toxin production. According to the Public Health Agency of Canada (PHAC), more than 30,000 cases of STEC infections occur each year in Canada (1). Environmentally, the main reservoir for STEC is cattle. Transmission of STEC to humans typically is associated with the consumption of contaminated food such as undercooked beef, fresh produce, unpasteurized milk, or contaminated drinking water (2), but these pathogens also can be transmitted from person to person or via direct contact with animals or their feces.The 2003 Karmali seropathotype model classifies STEC into seropathotypes based on their reported incidence in human disease, outbreaks, and/or association with the development of severe symptoms in humans (3). Serotypes frequently responsible for hemorrhagic colitis (HC) and HUS, ...

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Section: Discussionmentioning

confidence: 99%

Biofilm-Forming Abilities of Shiga Toxin-Producing Escherichia coli Isolates Associated with Human Infections

Vogeleer

Tremblay

Jubelin³

et al. 2016

Appl Environ Microbiol

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“…Early studies identified the type 1 fimbriae in the EHEC strains O26 and O118 (154) after having been genetically traced to other EHEC strains, including O157:H7, O157:H-, and O55- (155). Despite the presence of the coding regions in the genome of these strains, type 1 fimbriae expression was not observed in these EHEC strains.…”

Section: Other Fimbrial Adhesin Proteinsmentioning

confidence: 99%

Enterohemorrhagic Escherichia coli Adhesins

2014

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Adhesins are a group of proteins in enterohemorrhagic Escherichia coli (EHEC) that are involved in the attachment or colonization of this pathogen to abiotic (plastic or steel) and biological surfaces, such as those found in bovine and human intestines. This review provides the most up-to-date information on these essential adhesion factors, summarizing important historical discoveries and analyzing the current and future state of this research. In doing so, the proteins intimin and Tir are discussed in depth, especially regarding their role in the development of attaching and effacing lesions and in EHEC virulence. Further, a series of fimbrial proteins (Lpf1, Lpf2, curli, ECP, F9, ELF, Sfp, HCP, and type 1 fimbriae) are also described, emphasizing their various contributions to adherence and colonization of different surfaces and their potential use as genetic markers in detection and classification of different EHEC serotypes. This review also discusses the role of several autotransporter proteins (EhaA-D, EspP, Saa and Sab, and Cah), as well as other proteins associated with adherence, such as flagella, EibG, Iha, and OmpA. While these proteins have all been studied to varying degrees, all of the adhesins summarized in this chapter have been linked to different stages of the EHEC life cycle, making them good targets for the development of more effective diagnostics and therapeutics.

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Physical properties of the specific PapG–galabiose binding in E. coli P pili-mediated adhesion

et al. 2008

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Detailed analyses of the mechanisms that mediate binding of the uropathogenic Escherichia coli to host cells are essential, as attachment is a prerequisite for the subsequent infection process. We explore, by means of force measuring optical tweezers, the interaction between the galabiose receptor and the adhesin PapG expressed by P pili on single bacterial cells. Two variants of dynamic force spectroscopy were applied based on constant and non-linear loading force. The specific PapG-galabiose binding showed typical slip-bond behaviour in the force interval (30-100 pN) set by the pilus intrinsic biomechanical properties. Moreover, it was found that the bond has a thermodynamic off-rate and a bond length of 2.6 x 10(-3) s(-1) and 5.0 A, respectively. Consequently, the PapG-galabiose complex is significantly stronger than the internal bonds in the P pilus structure that stabilizes the helical chain-like macromolecule. This finding suggests that the specific binding is strong enough to enable the P pili rod to unfold when subjected to strong shear forces in the urinary tract. The unfolding process of the P pili rod promotes the formation of strong multipili interaction, which is important for the bacterium to maintain attachment to the host cells.

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Expression of type I pili is abolished in verotoxin-producingEscherichia coliO157

Cited by 25 publications

References 16 publications

Biofilm-Forming Abilities of Shiga Toxin-Producing Escherichia coli Isolates Associated with Human Infections

Biofilm-Forming Abilities of Shiga Toxin-Producing Escherichia coli Isolates Associated with Human Infections

Enterohemorrhagic Escherichia coli Adhesins

Physical properties of the specific PapG–galabiose binding in E. coli P pili-mediated adhesion

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