Ultrastructural and Biochemical Changes in Human Jejunal Mucosa Associated with Enteropathogenic Escherichia coli (0111) Infection

Ce, Taylor; Hart, A; Batt, R. M.; McDougall, Catherine; McLean, Lynn

doi:10.1097/00005176-198601000-00013

Cited by 54 publications

(48 citation statements)

References 0 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The role of these proteins in the EPEC FTTSS has already been covered, but EspB also appears to have other functions in EPEC virulence. After contact, the EspB protein is translocated into the host cell membrane (146), but it is also targeted to the host cell cytoplasm (173), where it has been proposed to act as a cytoskeletal toxin causing actin redistribution (174). A recent study of EHEC by using the two-hybrid system (109) has demonstrated that the N-terminal region of EspB interacts directly with the host cytoskeletal protein ␣-catenin.…”

Section: Epec Secreted Proteinsmentioning

confidence: 99%

“…It is proposed that the formation of AE lesions results in a reduction in the absorptive capacity of the intestinal mucosa, which inevitably leads to disruption of the electrolyte balance and subsequently to diarrhea. AE lesions have been demonstrated both in vivo (in biopsy specimens taken from infants with diarrhea) (24,148,173) and in vitro with a range of cell lines and organ explants (56,106,134). AE lesion formation is dependent on a number of physiological and environmental conditions (146) and is optimal in early to midlogarithmic growth at 37°C (AE lesions are not induced at 28°C).…”

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Virulence of EnteropathogenicEscherichia coli, a Global Pathogen

et al. 2003

View full text Add to dashboard Cite

Enteropathogenic Escherichia coli (EPEC) remains an important cause of diarrheal disease worldwide. Research into EPEC is intense and provides a good virulence model of other E. coli infections as well as other pathogenic bacteria. Although the virulence mechanisms are now better understood, they are extremely complex and much remains to be learnt. The pathogenesis of EPEC depends on the formation of an ultrastructural lesion in which the bacteria make intimate contact with the host apical enterocyte membrane. The formation of this lesion is a consequence of the ability of EPEC to adhere in a localized manner to the host cell, aided by bundle-forming pili. Tyrosine phosphorylation and signal transduction events occur within the host cell at the lesion site, leading to a disruption of the host cell mechanisms and, consequently, to diarrhea. These result from the action of highly regulated EPEC secreted proteins which are released via a type III secretion system, many genes of which are located within a pathogenicity island known as the locus of enterocyte effacement. Over the last few years, dramatic increases in our knowledge of EPEC virulence have taken place. This review therefore aims to provide a broad overview of and update to the virulence aspects of EPEC

show abstract

Section: Epec Secreted Proteinsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Virulence of EnteropathogenicEscherichia coli, a Global Pathogen

et al. 2003

View full text Add to dashboard Cite

show abstract

“…Studies in which bowel biopsies of infected infants have been examined have shown that EPEC bacteria adhere to the mucosa of the small and large bowel, and close attachment between EPEC and the small bowel mucosa has been demonstrated in many cases of EPEC diarrhea (37,54,169,170,188,198,205). In some cases, biopsies have not demonstrated EPEC adhering to the bowel (188).…”

Section: Pathophysiology Of Epec Infectionmentioning

confidence: 99%

Adhesion and its role in the virulence of enteropathogenic Escherichia coli

Law

1994

Clin Microbiol Rev

View full text Add to dashboard Cite

Enteropathogenic Escherichia coli (EPEC) organisms are an important cause of diarrheal disease in young children. The virulence of EPEC is a multifactorial process and involves a number of distinct stages. Initial adherence to intestinal mucosa is mediated by fimbriae which bring about a distinct form of adhesion, localized adhesion. Intimate adhesion of the bacterium to the eukaryotic membrane occurs, resulting in the activation of signal transduction pathways. Microvilli are disrupted and effaced from the apical membrane which then cups around the organism to form pedestal structures, the attaching and effacing lesion. Diarrhea may be produced by alteration of the permeability of the apical membrane and also through a malabsorption mechanism. The pathways involved in the production of the attaching and effacing lesion are described. EPEC organisms were originally thought to belong to a number of distinct serogroups; it is now apparent that many isolates belonging to these serogroups are not pathogenic or belong to other pathogenic groups of E. coli. In addition, isolates falling outside of these serogroups are considered to be true EPEC. The definition of EPEC based on serotyping is inaccurate and should be replaced by methods that specifically detect the virulence properties of EPEC.

show abstract

“…In 2011, one of the most prevalent diarrhea inducing pathogens, enteropathogenic Escherichia coli (EPEC), 4 caused an estimated 79,000 deaths in this age category of children (2). Following ingestion, EPEC adheres intimately to the epithelial cells of the small intestine and causes effacement of microvilli and formation of actin pedestals beneath the bacterium (3)(4)(5)(6). Once adhered to the intestinal epithelium, EPEC assembles a virulence-specific protein transport system (referred to as the type III secretion system or T3SS).…”

mentioning

confidence: 99%

Structural Analysis of a Specialized Type III Secretion System Peptidoglycan-cleaving Enzyme

Burkinshaw

Deng

Lameignère

et al. 2015

Journal of Biological Chemistry

View full text Add to dashboard Cite

Background: Bacterial virulence-associated type III secretion system (T3SS) assembly requires a dedicated enzyme to penetrate peptidoglycan (PG). Results: We structurally characterized a T3SS PG-lytic enzyme, identified catalytically important residues, and characterized its activity. Conclusion:The active site is similar to lysozymes and lytic transglycosylases and interaction with the T3SS enhances activity. Significance: Structural information is critical for development of drugs targeting T3SS PG-lytic enzymes.

show abstract

Ultrastructural and Biochemical Changes in Human Jejunal Mucosa Associated with Enteropathogenic Escherichia coli (0111) Infection

Cited by 54 publications

References 0 publications

Virulence of EnteropathogenicEscherichia coli, a Global Pathogen

Virulence of EnteropathogenicEscherichia coli, a Global Pathogen

Adhesion and its role in the virulence of enteropathogenic Escherichia coli

Structural Analysis of a Specialized Type III Secretion System Peptidoglycan-cleaving Enzyme

Contact Info

Product

Resources

About