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Open AccessJournal ArticleDOI

Role of Pore-Forming Toxins in Bacterial Infectious Diseases

TLDR
Common functions of PFTs include disruption of epithelial barrier function and evasion of host immune responses, which contribute to bacterial growth and spreading, make this group of toxins an attractive target for the development of new virulence-targeted therapies that may have broad activity against human pathogens.
Abstract
SUMMARY Pore-forming toxins (PFTs) are the most common bacterial cytotoxic proteins and are required for virulence in a large number of important pathogens, including Streptococcus pneumoniae, group A and B streptococci, Staphylococcus aureus, Escherichia coli, and Mycobacterium tuberculosis. PFTs generally disrupt host cell membranes, but they can have additional effects independent of pore formation. Substantial effort has been devoted to understanding the molecular mechanisms underlying the functions of certain model PFTs. Likewise, specific host pathways mediating survival and immune responses in the face of toxin-mediated cellular damage have been delineated. However, less is known about the overall functions of PFTs during infection in vivo . This review focuses on common themes in the area of PFT biology, with an emphasis on studies addressing the roles of PFTs in in vivo and ex vivo models of colonization or infection. Common functions of PFTs include disruption of epithelial barrier function and evasion of host immune responses, which contribute to bacterial growth and spreading. The widespread nature of PFTs make this group of toxins an attractive target for the development of new virulence-targeted therapies that may have broad activity against human pathogens.

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Journal ArticleDOI

Pore-forming toxins: ancient, but never really out of fashion

TL;DR: The diverse pore architectures and membrane insertion mechanisms that have been revealed by structural studies of PFTs are discussed, and how these features contribute to binding specificity for different membrane targets are considered.

Candidalysin is a Fungal Peptide Toxin Critical for Mucosal Infection and Immune Activation

TL;DR: This work identifies the first, to the authors' knowledge, fungal cytolytic peptide toxin in the opportunistic pathogen Candida albicans, which directly damages epithelial membranes, triggers a danger response signalling pathway and activates epithelial immunity.
Journal ArticleDOI

Virulence factors, prevalence and potential transmission of extraintestinal pathogenic Escherichia coli isolated from different sources: recent reports

TL;DR: The aim of this study was to characterize E. coli strains isolated from humans, animals and food for the presence of bacterial genes encoding virulence factors such as toxins, and iron acquisition systems in the context of an increasing spread of ExPEC infections.
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Bacillus thuringiensis and Its Pesticidal Crystal Proteins

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The pro- and anti-inflammatory properties of the cytokine interleukin-6

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Journal ArticleDOI

Structure of Staphylococcal α-Hemolysin, a Heptameric Transmembrane Pore

TL;DR: The structure proves the heptameric subunit stoichiometry of the α-hemolysin oligomer, shows that a glycine-rich and solvent-exposed region of a water-soluble protein can self-assemble to form a transmembrane pore of defined structure, and provides insight into the principles of membrane interaction and transport activity of β barrel pore-forming toxins.
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