Results 11 to 20 of about 1,369,932 (286)

Structural Insights into Clostridium perfringens Delta Toxin Pore Formation. [PDF]

open access: yesPLoS ONE, 2013
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
doaj   +2 more sources

Pore-forming toxins.

open access: yesCellular and Molecular Life Sciences, 2016
Pore-forming toxins are widely distributed proteins which form lesions in biological membranes. In this review, bacterial pore-forming toxins are treated as a paradigm and discussed in terms of the structural principles on which they work.

core   +4 more sources

Identification of a Key Residue for Oligomerisation and Pore-Formation of Clostridium perfringens NetB [PDF]

open access: yesToxins, 2014
Necrotic enteritis toxin B (NetB) is a β-pore-forming toxin produced by Clostridium perfringens and has been identified as a key virulence factor in the pathogenesis of avian necrotic enteritis, a disease causing significant economic damage to the ...
Sérgio P. Fernandes da Costa   +6 more
doaj   +2 more sources

Pore-forming activity of clostridial binary toxins

open access: yesBiochimica et Biophysica Acta (BBA) - Biomembranes, 2016
International audienceClostridial binary toxins (Clostridium perfringens Iota toxin, Clostridium difficile transferase, Clostridium spiroforme toxin, Clostridium botulinum C2 toxin) as Bacillus binary toxins, including Bacillus anthracis toxins consist ...
Popoff, Michel Robert   +2 more
core   +3 more sources

The Aerolysin-Like Toxin Family of Cytolytic, Pore-Forming Toxins [PDF]

open access: yesThe Open Toxinology Journal, 2010
International audiencePore-forming toxins (PFTs) represent the largest known group of bacterial protein toxins to date. Membrane insertion and subsequent pore-formation occurs after initial binding to cell-surface receptor and oligomerization. Aerolysin,
Popoff, Michel   +2 more
core   +2 more sources

Structural and Functional Analysis of the Pore-Forming Toxin NetB from Clostridium perfringens [PDF]

open access: yesmBio, 2013
Clostridium perfringens is an anaerobic bacterium that causes numerous important human and animal diseases, primarily as a result of its ability to produce many different protein toxins. In chickens, C. perfringens causes necrotic enteritis, a disease of
Xu-Xia Yan   +13 more
doaj   +2 more sources

V. cholerae MakA is a cholesterol-binding pore-forming toxin that induces non-canonical autophagy. [PDF]

open access: yesJ Cell Biol, 2022
Pore-forming toxins (PFTs) are important virulence factors produced by many pathogenic bacteria. Here, we show that the Vibrio cholerae toxin MakA is a novel cholesterol-binding PFT that induces non-canonical autophagy in a pH-dependent manner.
Jia X   +8 more
europepmc   +2 more sources

Current Perspective on the Membrane-Damaging Action of Thermostable Direct Hemolysin, an Atypical Bacterial Pore-forming Toxin. [PDF]

open access: yesFront Mol Biosci, 2021
Thermostable direct hemolysin (TDH) is the major virulence determinant of the gastroenteric bacterial pathogen Vibrio parahaemolyticus. TDH is a membrane-damaging pore-forming toxin (PFT).
Verma P, Chattopadhyay K.
europepmc   +2 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

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

open access: yesProc 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
Vögele M   +7 more
europepmc   +8 more sources

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