Anthrax toxin-induced rupture of artificial lipid bilayer membranes

Nablo, Brian J.; Panchal, Rekha G.; Bavari, Sina; Nguyen, Tam Luong; Gussio, Rick; Ribot, Wilson J.; Friedlander, A. M.; Chabot, Donald J.; Reiner, Joseph E.; Robertson, Joseph W. F.; Balijepalli, Arvind; Halverson, Kelly M.; Kasianowicz, John J.

doi:10.1063/1.4816467

Cited by 18 publications

(41 citation statements)

References 128 publications

(158 reference statements)

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“…However, an alternative model has been proposed based on membrane rupture. Using artificial lipid bilayers and physiological pH gradient (5.5/7/2) of endosomal acidification, it has been observed that LF or EF irreversibly binds to PA channels leading to disruption of the membrane and release of PA-LF or PA-EF complexes which are enzymatically active [116].…”

Section: Accepted Manuscriptmentioning

confidence: 99%

Pore-forming activity of clostridial binary toxins

Knapp

Benz

Popoff

2016

Biochimica et Biophysica Acta (BBA) - Biomembranes

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Clostridial 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 of two independent proteins, one being the binding component which mediates the internalization into cell of the intracellularly active component. Clostridial binary toxins induce actin cytoskeleton disorganization through mono-ADP-ribosylation of globular actin and are responsible for enteric diseases. Clostridial and Bacillus binary toxins share structurally and functionally related binding components which recognize specific cell receptors, oligomerize, form pores in endocytic vesicle membrane, and mediate the transport of the enzymatic component into the cytosol. Binding components retain the global structure of pore-forming toxins (PFTs) from the cholesterol-dependent cytotoxin family such as perfringolysin. However, their pore-forming activity notably that of clostridial binding components is more related to that of heptameric PFT family including aerolysin and C. perfringens epsilon toxin. This review focuses upon pore-forming activity of clostridial binary toxins compared to other related PFTs. This article is part of a Special Issue entitled: Pore-Forming Toxins edited by Mauro Dalla Serra and Franco Gambale.

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Section: Accepted Manuscriptmentioning

confidence: 99%

Pore-forming activity of clostridial binary toxins

Knapp

Benz

Popoff

2016

Biochimica et Biophysica Acta (BBA) - Biomembranes

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“…On the other hand, the host cell chaperones Hsp90 and the peptidyl-prolyl cis/trans isomerase cyclophilin A were reported to be critical for membrane translocation of the active moieties of clostridial C2, iota, and CDT toxins but not for LF of the anthrax toxin [368,369,370]. Provided that the corresponding bilayer measurements show successful translocation events similar to those described for the anthrax toxin, we believe these findings would add some useful arguments to the anthrax toxin uptake debate [18]. For that purpose, not only the native but also the PA 63 /C2I-His cross-combination of components could be tested.…”

Section: Discussionmentioning

confidence: 92%

Channel-Forming Bacterial Toxins in Biosensing and Macromolecule Delivery

Gurnev

Nestorovich

2014

Toxins

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To intoxicate cells, pore-forming bacterial toxins are evolved to allow for the transmembrane traffic of different substrates, ranging from small inorganic ions to cell-specific polypeptides. Recent developments in single-channel electrical recordings, X-ray crystallography, protein engineering, and computational methods have generated a large body of knowledge about the basic principles of channel-mediated molecular transport. These discoveries provide a robust framework for expansion of the described principles and methods toward use of biological nanopores in the growing field of nanobiotechnology. This article, written for a special volume on “Intracellular Traffic and Transport of Bacterial Protein Toxins”, reviews the current state of applications of pore-forming bacterial toxins in small- and macromolecule-sensing, targeted cancer therapy, and drug delivery. We discuss the electrophysiological studies that explore molecular details of channel-facilitated protein and polymer transport across cellular membranes using both natural and foreign substrates. The review focuses on the structurally and functionally different bacterial toxins: gramicidin A of Bacillus brevis, α-hemolysin of Staphylococcus aureus, and binary toxin of Bacillus anthracis, which have found their “second life” in a variety of developing medical and technological applications.

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“…To answer the fundamental question regarding the origin of the protein translocation driving force, the authors suggest that the PA 63 symporter achieves protein translocation using a tandem of two synergistic Brownian ratchets: the ϕ-clamp ratchet, promoting the substrate unfolding, and the charge-state ratchet, which biases the entry rates of the substrates into the pore. A conceptually different model of anthrax toxin translocation was recently suggested by Nablo and colleagues [46]. The model proposes that instead of the active components being threaded through the pore, anthrax toxin complexes (namely, LF or EF bound to the PA 63 channel) rupture membranes.…”

Section: Anthrax Toxin Of B Anthracismentioning

confidence: 98%