Structural Basis of the Pore-Forming Toxin/Membrane Interaction [PDF]
Toxins, 2021 With the rapid growth of antibiotic-resistant bacteria, it is urgent to develop alternative therapeutic strategies. Pore-forming toxins (PFTs) belong to the largest family of virulence factors of many pathogenic bacteria and constitute the most ...
Yajuan Li +9 more
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Curcumin Inhibits Membrane-Damaging Pore-Forming Function of the β-Barrel Pore-Forming Toxin Vibrio cholerae Cytolysin [PDF]
Frontiers in Microbiology, 2022 Vibrio cholerae cytolysin (VCC) is a β-barrel pore-forming toxin (β-PFT). Upon encountering the target cells, VCC forms heptameric β-barrel pores and permeabilizes the cell membranes.
Mahendra Singh +3 more
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Temporary Membrane Permeabilization via the Pore-Forming Toxin Lysenin [PDF]
Toxins, 2020 Pore-forming toxins are alluring tools for delivering biologically-active, impermeable cargoes to intracellular environments by introducing large conductance pathways into cell membranes.
Nisha Shrestha +8 more
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Membrane perforation by the pore-forming toxin pneumolysin. [PDF]
Proc Natl Acad Sci U S A, 2019 Significance Pneumolysin, a pore-forming toxin of Streptococcus pneumoniae , assembles into rings on cholesterol-containing membranes of host cells. β -hairpins form a barrel-shaped transmembrane
Vögele M +7 more
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Structure and mechanism of the two-component α-helical pore-forming toxin YaxAB [PDF]
Nature Communications, 2018 The Yersinia YaxAB system is a pore-forming toxin of so far unknown structure. Here authors present X-ray and cryo-EM to structures of individual subunits and of the YaxAB pore complex, and find that YaxA binds to membranes first and recruits YaxB for ...
Bastian Bräuning +9 more
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Host glycan recognition by a pore forming toxin. [PDF]
Structure, 2012 An exposed F-type lectin domain fused to the N-terminus of a cholesterol-dependent cytolysin scaffold allows Streptococcus mitis lectinolysin to cluster at fucose-rich sites on target cell membranes, thereby leading to increased pore-forming toxin activity.
Bouyain S, Geisbrecht BV.
europepmc +4 more sources
Complete structures of the YenTc holotoxin prepore and pore reveal the evolutionary basis for chitinase incorporation into ABC toxins [PDF]
Nature CommunicationsABC toxins are toxin-translocating, pore-forming proteins found in a wide range of insecticidal bacteria and some mammalian pathogens. The Yersinia entomopahaga toxin complex (YenTc) belongs to a distinct subclass of ABC toxins, defined by a divergent ...
Yu Shang Low +13 more
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Bacterial pore-forming toxins.
Microbiology (Reading, England), 2022 Pore-forming toxins (PFTs) are widely distributed in both Gram-negative and Gram-positive bacteria. PFTs can act as virulence factors that bacteria utilise in dissemination and host colonisation or, alternatively, they can be employed to compete with rival microbes in polymicrobial niches. PFTs transition from a soluble form to become membrane-embedded
Ulhuq, Fatima R., Mariano, Giuseppina
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Alciporin, a pore-forming protein as complementary defense mechanism in Millepora alcicornis
Frontiers in Marine Science, 2022 Millepora alcicornis (Cnidaria: Hydrozoa), known as fire coral, is a tropical species settled in marine ecosystems of the Canary Islands in the last years.
Nathalia Nocchi +13 more
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Pore‐forming toxins of foodborne pathogens [PDF]
Comprehensive Reviews in Food Science and Food Safety, 2021 Abstract Pore‐forming toxins (PFTs) are water‐soluble molecules that have been identified as the most crucial virulence factors during bacterial pathogenesis. PFTs disrupt the host cell membrane to internalize or to deliver other bacterial or virulence factors for establishing infections.
Rajashri Banerji +3 more
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