Results 1 to 10 of about 33,852 (156)

Structural Basis of the Pore-Forming Toxin/Membrane Interaction [PDF]

open access: yesToxins, 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
doaj   +9 more sources

Membrane perforation by the pore-forming toxin pneumolysin [PDF]

open access: yesProceedings of the National Academy of Sciences of the United States of America, 2019
Significance Pneumolysin, a pore-forming toxin of Streptococcus pneumoniae , assembles into rings on cholesterol-containing membranes of host cells. β
Gerhard Hummer   +2 more
exaly   +9 more sources

Curcumin Inhibits Membrane-Damaging Pore-Forming Function of the β-Barrel Pore-Forming Toxin Vibrio cholerae Cytolysin [PDF]

open access: yesFrontiers 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
doaj   +2 more sources

Temporary Membrane Permeabilization via the Pore-Forming Toxin Lysenin [PDF]

open access: yesToxins, 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
doaj   +2 more sources

Structure and mechanism of the two-component α-helical pore-forming toxin YaxAB [PDF]

open access: yesNature 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
doaj   +2 more sources

Alciporin, a pore-forming protein as complementary defense mechanism in Millepora alcicornis

open access: yesFrontiers 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
doaj   +1 more source

Bacterial pore-forming toxins.

open access: yesMicrobiology (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
openaire   +4 more sources

Pore‐forming toxins of foodborne pathogens [PDF]

open access: yesComprehensive 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
openaire   +2 more sources

Programmed cellular necrosis mediated by the pore-forming alpha-toxin from Clostridium septicum. [PDF]

open access: yesPLoS Pathogens, 2009
Programmed necrosis is a mechanism of cell death that has been described for neuronal excitotoxicity and ischemia/reperfusion injury, but has not been extensively studied in the context of exposure to bacterial exotoxins.
Catherine L Kennedy   +4 more
doaj   +1 more source

Identification and validation of a linear protective neutralizing epitope in the β-pore domain of alpha toxin. [PDF]

open access: yesPLoS ONE, 2015
The plethora of virulence factors associated with Staphylococcus aureus make this bacterium an attractive candidate for a molecularly-designed epitope-focused vaccine.
Jon Oscherwitz, Kemp B Cease
doaj   +1 more source

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