Nature. J. Biol. doi: 10.1128/JVI.01848-17. Once inside, the complex is transferred to an acidic compartment, where the heptamer, still in the non-membrane-spanning pre-pore conformation, is prepared for translocation of EF and LF into the cytosol.At first glance, the primary sequence of PA does not look like that of a membrane-spanning protein. 2018 Feb 26;92(6):e01848-17. They can be classified as Type III toxins because they interfere with internal cell function. Structures for the toxin molecules (Figs. 2020 Jun 23;10:214. doi: 10.3389/fcimb.2020.00214. Epub 2009 Jun 27.Santelli E, Bankston LA, Leppla SH, Liddington RC.Nature. doi: 10.15252/embj.2019101996. Acad.

A.; Collier, R. J. 2012, 21(5):606-24.Abrami, L.; Liu, S.; Cosson, P.; Leppla, S. H.; van der Goot, F. G. Anthrax toxin triggers endocytosis of its receptor via a lipid raft-mediated clathrin-dependent process. Nat Struct Mol Biol.
The catalytic factors also undergo dramatic structural changes as they unfold to allow for their translocation across the endosomal membrane and refold to preserve their catalytic activity within the cytosol. eCollection 2020.Xu H, Shi J, Gao H, Liu Y, Yang Z, Shao F, Dong N.EMBO J. Lacy DB(1), Collier RJ. In the presence of a host cell-surface receptor, PA can mediate the delivery of EF and LF from the extracellular milieu into the host cell cytosol to effect toxicity.
"/> Nature. J. Biol. doi: 10.1128/JVI.01848-17. Once inside, the complex is transferred to an acidic compartment, where the heptamer, still in the non-membrane-spanning pre-pore conformation, is prepared for translocation of EF and LF into the cytosol.At first glance, the primary sequence of PA does not look like that of a membrane-spanning protein. 2018 Feb 26;92(6):e01848-17. They can be classified as Type III toxins because they interfere with internal cell function. Structures for the toxin molecules (Figs. 2020 Jun 23;10:214. doi: 10.3389/fcimb.2020.00214. Epub 2009 Jun 27.Santelli E, Bankston LA, Leppla SH, Liddington RC.Nature. doi: 10.15252/embj.2019101996. Acad.

A.; Collier, R. J. 2012, 21(5):606-24.Abrami, L.; Liu, S.; Cosson, P.; Leppla, S. H.; van der Goot, F. G. Anthrax toxin triggers endocytosis of its receptor via a lipid raft-mediated clathrin-dependent process. Nat Struct Mol Biol.
The catalytic factors also undergo dramatic structural changes as they unfold to allow for their translocation across the endosomal membrane and refold to preserve their catalytic activity within the cytosol. eCollection 2020.Xu H, Shi J, Gao H, Liu Y, Yang Z, Shao F, Dong N.EMBO J. Lacy DB(1), Collier RJ. In the presence of a host cell-surface receptor, PA can mediate the delivery of EF and LF from the extracellular milieu into the host cell cytosol to effect toxicity.
"> Nature. J. Biol. doi: 10.1128/JVI.01848-17. Once inside, the complex is transferred to an acidic compartment, where the heptamer, still in the non-membrane-spanning pre-pore conformation, is prepared for translocation of EF and LF into the cytosol.At first glance, the primary sequence of PA does not look like that of a membrane-spanning protein. 2018 Feb 26;92(6):e01848-17. They can be classified as Type III toxins because they interfere with internal cell function. Structures for the toxin molecules (Figs. 2020 Jun 23;10:214. doi: 10.3389/fcimb.2020.00214. Epub 2009 Jun 27.Santelli E, Bankston LA, Leppla SH, Liddington RC.Nature. doi: 10.15252/embj.2019101996. Acad.

A.; Collier, R. J. 2012, 21(5):606-24.Abrami, L.; Liu, S.; Cosson, P.; Leppla, S. H.; van der Goot, F. G. Anthrax toxin triggers endocytosis of its receptor via a lipid raft-mediated clathrin-dependent process. Nat Struct Mol Biol.
The catalytic factors also undergo dramatic structural changes as they unfold to allow for their translocation across the endosomal membrane and refold to preserve their catalytic activity within the cytosol. eCollection 2020.Xu H, Shi J, Gao H, Liu Y, Yang Z, Shao F, Dong N.EMBO J. Lacy DB(1), Collier RJ. In the presence of a host cell-surface receptor, PA can mediate the delivery of EF and LF from the extracellular milieu into the host cell cytosol to effect toxicity.
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Anthrax toxin structure

by


Petosa et al.

Structures With Same Primary Citation.

2006, 281, 1630–1635.Feld GK, Brown MJ, Krantz BA. Users can perform simple and advanced searches based on annotations relating to sequence, structure and function. Download high quality TIFF image. Anthrax toxin is a binary A-B toxin comprised of protective antigen (PA) and two enzymatic moieties, edema factor (EF) and lethal factor (LF). These proteinsconsi… Nature. This binding occurs because after removing the PA20 domain, a large hydrophobic surface is uncovered on domain 1 of PA63. Proc. Domain 1 provides a large surface that the interacts with the N-terminus of EF and LF.Upon formation of the prepore and attachment of LF and/or EF, the heptamer migrates to a lipid raft where it is rapidly endocytosed.As discussed, each molecule interacts with several others in order to induce the endocytosis of the anthrax toxin.

The molecular interactions are apparent upon performing a detailed analysis of the structures of PA, EF, LF, and the cellular receptors (ANTXR1 and ANTXR2). Sci. 2009 Jan;18(1):17-23. doi: 10.1002/pro.26.Younes S, Al-Sulaiti A, Nasser EAA, Najjar H, Kamareddine L.Front Cell Infect Microbiol. The first step after endocytosis is the acidification of the endocytotic vesicle. Cell Biol. Structure of anthrax toxin PA in complex with the headpiece of a host cellular receptor CMG2. The acidification plays two roles in the lifespan of the toxin. In the presence of a host cell-surface receptor, PA can mediate the delivery of … Author information: (1)Department of Microbiology and Molecular Genetics, Harvard Medical School, Boston, MA 02115, USA. Prot Sci. In order for LF and EF to function inside a target cell, they must localize to the cell and enter its cytoplasm. PubMed Abstract: After binding to cellular receptors and proteolytic activation, the protective antigen component of anthrax toxin forms a heptameric prepore. Structure and function of anthrax toxin. 2003, 160, 321–328.Mourez, M. Anthrax toxins. Upon examination of the structure of domain 2 (Fig. proposed a model of how this occurs.PA is endocytosed as a soluble heptamer attached to its receptors, with LF or EF attached to the heptamer as cargo. The molecular interactions are apparent upon performing a detailed analysis of the structures of PA, EF, LF, and the cellular receptors (.The structure of PA was the first to be determined (Fig. Chem. Each individual anthrax toxin protein is nontoxic. 10) also built a hypothetical structure of the membrane-inserted PA/CMG2 structure. The hypothesis can be examined with molecular dynamics simulations that provide important structural insights into the pore-formation mechanism. One of these proteins, protective antigen (PA), transports the other two, edema factor (EF) and lethal factor (LF), to the cytosol. LF and EF are pH sensitive, and as the pH drops, their structures lose stability. The lumen on the PA63 pore is only 15 Å (1.5 nm) across, which is much smaller than the diameter of LF or EF. 2000 Apr;68(4):1781-6. doi: 10.1128/iai.68.4.1781-1786.2000.Rajapaksha M, Eichler JF, Hajduch J, Anderson DE, Kirk KL, Bann JG.Protein Sci. CMG2 provides additional support to the pore.Several recent studies demonstrate how the PA63 pore allows the EF and LF into the cytoplasm when its lumen is so small. These molecules are visualized, downloaded, and analyzed by users who range from students to specialized scientists. The mechanism of anthrax toxin action is the result of the molecular structures of the three toxin proteins in combination with biomolecules of the host cell. 3).Petosa et al. 2004, 430, 905–908.Feld GK, Thoren KL, Kintzer AF, Sterling HJ, Tang II, Greenberg SG, Williams ER, Krantz BA. Structural Determinates for the Binding of Anthrax Lethal Factor to Oligomeric Protective Antigen.

The "A" subunit possesses enzyme activity, and is transferred to the host cell following a conformational change in the membrane-bound transport "B" subunit. Translocation occurs through a series of events which begin in the endosome as it acidifies. Biochem. 2019 Jul 1;38(13):e101996. Anthrax toxin is the major virulence factor secreted by Bacillus anthracis, causing high mortality in humans and other mammals. 2018 Dec 10;18(1):640. doi: 10.1186/s12879-018-3542-6.J Virol. Please enable it to take advantage of the complete set of features!Clipboard, Search History, and several other advanced features are temporarily unavailable.National Center for Biotechnology Information,Unable to load your collection due to an error,Unable to load your delegates due to an error.Mol Aspects Med.
Nature. J. Biol. doi: 10.1128/JVI.01848-17. Once inside, the complex is transferred to an acidic compartment, where the heptamer, still in the non-membrane-spanning pre-pore conformation, is prepared for translocation of EF and LF into the cytosol.At first glance, the primary sequence of PA does not look like that of a membrane-spanning protein. 2018 Feb 26;92(6):e01848-17. They can be classified as Type III toxins because they interfere with internal cell function. Structures for the toxin molecules (Figs. 2020 Jun 23;10:214. doi: 10.3389/fcimb.2020.00214. Epub 2009 Jun 27.Santelli E, Bankston LA, Leppla SH, Liddington RC.Nature. doi: 10.15252/embj.2019101996. Acad.

A.; Collier, R. J. 2012, 21(5):606-24.Abrami, L.; Liu, S.; Cosson, P.; Leppla, S. H.; van der Goot, F. G. Anthrax toxin triggers endocytosis of its receptor via a lipid raft-mediated clathrin-dependent process. Nat Struct Mol Biol.
The catalytic factors also undergo dramatic structural changes as they unfold to allow for their translocation across the endosomal membrane and refold to preserve their catalytic activity within the cytosol. eCollection 2020.Xu H, Shi J, Gao H, Liu Y, Yang Z, Shao F, Dong N.EMBO J. Lacy DB(1), Collier RJ. In the presence of a host cell-surface receptor, PA can mediate the delivery of EF and LF from the extracellular milieu into the host cell cytosol to effect toxicity.

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