Results 11 to 20 of about 33,951 (255)
Pore-Forming Toxins Trigger the Purge [PDF]
The intestinal epithelium responds to pathogens by coordinating microbial elimination with tissue repair, both required to survive an infection. In this issue of Cell Host & Microbe, Lee et al. (2016) discover a rapid and evolutionarily conserved response to pore-forming toxins in the gut, involving cytoplasm ejection and enterocyte regrowth.
Alessandro, Bonfini, Nicolas, Buchon
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Enhanced SnapShot: Pore-Forming Toxins [PDF]
Enhanced SnapShots include features only possible online—animations, embedded captions, and dynamic visuals—all accessible by the click of a mouse. The goal of an Enhanced SnapShot is to provide everything currently available with the print SnapShot plus additional layers of information that are accessible through an easy to navigate interface.The ...
Mueller M, Ban N
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Membrane Permeabilization by Pore-Forming RTX Toxins: What Kind of Lesions Do These Toxins Form?
Pore-forming toxins (PFTs) form nanoscale pores across target membranes causing cell death. The pore-forming cytolysins of the RTX (repeats in toxin) family belong to a steadily increasing family of proteins characterized by having in their primary ...
Helena Ostolaza +5 more
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Cryo-EM structures of an insecticidal Bt toxin reveal its mechanism of action on the membrane
The Vip3 family proteins from Bacillus thuringiensis are thought to exert their insecticidal activity through pore formation. Here authors present cryo-EM structures of a Vip3 family toxin in both inactive and activated forms and show the activated ...
Matthew J. Byrne +9 more
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The Pore-forming Toxin Proaerolysin Is Activated by Furin [PDF]
Aerolysin is secreted as an inactive dimeric precursor by the bacterium Aeromonas hydrophila. Proteolytic cleavage within a mobile loop near the C terminus of the protoxin is required for oligomerization and channel formation. This loop contains the sequence KVRRAR432, which should be recognized by mammalian proprotein convertases such as furin, PACE4,
Abrami, L. +8 more
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The pore structure of Clostridium perfringens epsilon toxin
Epsilon toxin (Etx) is a potent pore forming toxin (PFT) produced by Clostridium perfringens. Here authors show the cryo-EM structure of the Etx pore assembled on the membrane of susceptible cells and shed light on pore formation and mutant phenotypes.
Christos G. Savva +7 more
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DEFENSE AND DEATH RESPONSES TO PORE FORMING TOXINS [PDF]
Pore forming toxins (PFT) are important virulence factors produced by bacteria to kill eukaryotic cells by forming holes in the cellular membrane. They represent a diverse group of proteins with a wide range of target cells. Although the amino acid sequence is not conserved among the different PFT, many of them share some aspects of their mechanism of ...
Angeles, Cancino-Rodezno +3 more
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Repair of a Bacterial Small β-Barrel Toxin Pore Depends on Channel Width
Membrane repair emerges as an innate defense protecting target cells against bacterial pore-forming toxins. Here, we report the first paradigm of Ca2+-dependent repair following attack by a small β-pore-forming toxin, namely, plasmid-encoded phobalysin ...
Gisela von Hoven +7 more
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Modular bacteriocins represent a major group of secreted protein toxins with a narrow spectrum of activity, involved in interference competition between Gram-negative bacteria.
Maarten G. K. Ghequire +4 more
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Structural Insights into Clostridium perfringens Delta Toxin Pore Formation.
Clostridium perfringens Delta toxin is one of the three hemolysin-like proteins produced by C. perfringens type C and possibly type B strains. One of the others, NetB, has been shown to be the major cause of Avian Nectrotic Enteritis, which following the
Jessica Huyet +5 more
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