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.read more
Citations
More filters
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.
Journal ArticleDOI
Candidalysin is a fungal peptide toxin critical for mucosal infection
David L. Moyes,Duncan Wilson,Jonathan P. Richardson,Selene Mogavero,Shirley X. Tang,Julia Wernecke,Sarah Höfs,Remi L. Gratacap,Jon Robbins,Manohursingh Runglall,Celia Murciano,Mariana Blagojevic,Selvam Thavaraj,Toni M. Förster,Betty Hebecker,Lydia Kasper,Gema Vizcay,Simona Ioana Iancu,Nessim Kichik,Nessim Kichik,Antje Häder,Oliver Kurzai,Ting Luo,Thomas Krüger,Olaf Kniemeyer,Ernesto Cota,Oliver Bader,Robert T. Wheeler,Thomas Gutsmann,Bernhard Hube,Julian R. Naglik +30 more
TL;DR: A fungal cytolytic peptide toxin in the opportunistic pathogen Candida albicans was identified in this article, which directly damages epithelial membranes, triggers a danger response signalling pathway and activates epithelial immunity.
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
Aggregatibacter actinomycetemcomitans–induced hypercitrullination links periodontal infection to autoimmunity in rheumatoid arthritis
Maximilian F. Konig,Loreto Abusleme,Jesper Reinholdt,Robert J. Palmer,Ricardo Teles,Ricardo Teles,Kevon Sampson,Antony Rosen,Peter A. Nigrovic,Peter A. Nigrovic,Jeremy Sokolove,Jon T. Giles,Niki M. Moutsopoulos,Felipe Andrade +13 more
TL;DR: It is demonstrated that a particular periodontal pathogen called Aggregatibacter actinomycetemcomitans (Aa) induces changes in neutrophil function, including hypercitrullination of host proteins, an abnormality that is also observed in the joints of patients with rheumatoid arthritis.
Journal ArticleDOI
Virulence factors, prevalence and potential transmission of extraintestinal pathogenic Escherichia coli isolated from different sources: recent reports
Jolanta Sarowska,Bożena Futoma-Kołoch,Agnieszka Jama-Kmiecik,Magdalena Frej-Madrzak,Marta Ksiazczyk,Gabriela Bugla-Płoskońska,Irena Choroszy-Król +6 more
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.
References
More filters
Journal ArticleDOI
Pathogen Recognition and Innate Immunity
TL;DR: New insights into innate immunity are changing the way the way the authors think about pathogenesis and the treatment of infectious diseases, allergy, and autoimmunity.
Journal ArticleDOI
Bacillus thuringiensis and Its Pesticidal Crystal Proteins
E. Schnepf,Neil Crickmore,J. Van Rie,Didier Lereclus,J. Baum,Jerald S. Feitelson,Daniel R. Zeigler,Donald H. Dean +7 more
TL;DR: Researchers are reporting promising results in engineering more-useful toxins and formulations, in creating transgenic plants that express pesticidal activity, and in constructing integrated management strategies to insure that these products are utilized with maximum efficiency and benefit.
Journal ArticleDOI
Studies on the Chemical Nature of the Substance Inducing Transformation of Pneumococcal Types: Induction of Transformation by a Desoxyribonucleic Acid Fraction Isolated from Pneumococcus Type III
TL;DR: A reprint of Avery, MacLeod, and McCarty's article on the 35th anniversary of its original publication.
Journal ArticleDOI
The pro- and anti-inflammatory properties of the cytokine interleukin-6
TL;DR: It turns out that regenerative or anti-inflammatory activities of interleukin-6 are mediated by classic signaling whereas pro-inflammatory responses of interLEukin -6 are rather mediated by trans-signaling.
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.