A Filterable Hæmolysin from Escherichia coli

Lovell, R.; Rees, T.A.

doi:10.1038/188755b0

Cited by 32 publications

(16 citation statements)

References 2 publications

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“…Pore-forming toxins belonging to the RTX family have previously been found in a wide variety of Gram-negative bacteria including E. coli (HlyA), Legionella (RtxA), Bordetella pertussis (CyaA) , Proteus (HlyA), Morganella (HlyA), Vibrio cholera (Rtx) and Actinobacillus pleuropneumoniae (ApxI, ApxII and ApXIII) [49–53]. These toxins form pores in cell membranes, which lose their function as barrier [54].…”

Section: Discussionmentioning

confidence: 99%

Pore forming activity of the potent RTX-toxin produced by pediatric pathogen Kingella kingae: Characterization and comparison to other RTX-family members

Bárcena-Uribarri

Benz

Winterhalter

et al. 2015

Biochimica et Biophysica Acta (BBA) - Biomembranes

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Pediatric septic arthritis in patients under age of four is frequently caused by the oral Gram-negative bacterium Kingella kingae. This organism may be responsible for a severe form of infective endocarditis in otherwise healthy children and adults. A major virulence factor of K. kingae is RtxA, a toxin that belongs to the RTX (Repeats-in-ToXin) group of secreted pore forming toxins. To understand the RtxA effects on host cell membranes, the toxin activity was studied using planar lipid bilayers. K. kingae strain PYKK081 and its isogenic RtxA-deficient strain, KKNB100, were tested for their ability to form pores in artificial membranes of asolectin/n-decane. RtxA, purified from PYKK081, was able to rapidly form pores with an apparent diameter of 1.9 nm as measured by the partition of nonelectrolytes in the pores. The RtxA channels are cation-selective and showed strong voltage-dependent gating. In contrast to supernatants of PYKK081, those of KKNB100 did not show any pore forming activity. We concluded that RtxA toxin is the only secreted protein from K. kingae forming large channels in host cell membranes where it induces cation flux leading to programmed cell death. Furthermore, our findings suggested that the planar lipid bilayer technique can effectively be used to test possible inhibitors of RTX toxin activity and to investigate the mechanism of the toxin binding to the membrane.

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Section: Discussionmentioning

confidence: 99%

Pore forming activity of the potent RTX-toxin produced by pediatric pathogen Kingella kingae: Characterization and comparison to other RTX-family members

Bárcena-Uribarri

Benz

Winterhalter

et al. 2015

Biochimica et Biophysica Acta (BBA) - Biomembranes

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“…In the 1960s, it was conclusively demonstrated that hemolysis was mediated by a labile, secreted molecule subsequently dubbed ‘α-hemolysin’ (HlyA) [22–24]. During the following decades, the genes responsible for secretion and activation of HlyA were identified, cloned and used to fulfill molecular Koch’s postulates in certain experimental systems, demonstrating that HlyA was in fact a bona fide virulence factor [25,26].…”

Section: α-Hemolysin: a Prototype Rtx Toxinmentioning

confidence: 99%

The RTX Pore-Forming Toxin α-Hemolysin of Uropathogenic Escherichia Coli : Progress and Perspectives

Wiles

Mulvey

2012

Future Microbiol.

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Members of the RTX family of protein toxins are functionally conserved among an assortment of bacterial pathogens. By disrupting host cell integrity through their pore-forming and cytolytic activities, this class of toxins allows pathogens to effectively tamper with normal host cell processes, promoting pathogenesis. Here, we focus on the biology of RTX toxins by describing salient properties of a prototype member, α-hemolysin, which is of ten encoded by strains of uropathogenic Escherichia coli. It has long been appreciated that RTX toxins can have distinct effects on host cells aside from outright lysis. Recently, advances in modeling and analysis of host–pathogen interactions have led to novel findings concerning the consequences of pore formation during host–pathogen interactions. We discuss current progress on longstanding questions concerning cell specificity and pore formation, new areas of investigation that involve toxin-mediated perturbations of host cell signaling cascades and perspectives on the future of RTX toxin investigation.

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“…Certain strains of E. coli are hemolytic (120,203), and, as this property is usually possessed by certain serotypes pathogenic for pigs, it is used to facilitate their isolation and identification.…”

Section: Identification and Classification Of The E Coli Groupmentioning

confidence: 99%

Escherichia coli and Neonatal Disease of Calves

Gay¹

1965

Bacteriological Reviews

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A Filterable Hæmolysin from Escherichia coli

Cited by 32 publications

References 2 publications

Pore forming activity of the potent RTX-toxin produced by pediatric pathogen Kingella kingae: Characterization and comparison to other RTX-family members

Pore forming activity of the potent RTX-toxin produced by pediatric pathogen Kingella kingae: Characterization and comparison to other RTX-family members

The RTX Pore-Forming Toxin α-Hemolysin of Uropathogenic Escherichia Coli : Progress and Perspectives

Escherichia coli and Neonatal Disease of Calves

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