ArticleMolecular microbiology2011
GRP78(BiP) facilitates the cytosolic delivery of anthrax lethal factor (LF) in vivo and functions as an unfoldase in vitro.
Article in Molecular microbiology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 20 citations in OpenAlex.
- GRP78 in human diseases: From molecular chaperone to therapeutic target.Theranostics · 2026Review
- ER residential chaperone GRP78 unconventionally relocalizes to the cell surface via endosomal transport.Cellular and molecular life sciences : CMLS · 2021Article
- Cryo-EM structure of the fully-loaded asymmetric anthrax lethal toxin in its heptameric pre-pore state.PLoS pathogens · 2020Article
- Lethal Factor Domain-Mediated Delivery of Nurr1 Transcription Factor Enhances Tyrosine Hydroxylase Activity and Protects from Neurotoxin-Induced Degeneration of Dopaminergic Cells.Molecular neurobiology · 2019Article
- Structure of anthrax lethal toxin prepore complex suggests a pathway for efficient cell entry.The Journal of general physiology · 2016Article
- Tumor Targeting and Drug Delivery by Anthrax Toxin.Toxins · 2016Review
- Article
- Polylysine-mediated translocation of the diphtheria toxin catalytic domain through the anthrax protective antigen pore.Biochemistry · 2014Article
- CCT chaperonin complex is required for efficient delivery of anthrax toxin into the cytosol of host cells.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- BiP negatively affects ricin transport.Toxins · 2013Article
- Article
- Bacillus anthracis edema factor substrate specificity: evidence for new modes of action.Toxins · 2012Review
- From structure to solutions: the role of basic research in developing anthrax countermeasures: Microbiology Graduate Program Seminar: Anthrax toxin.The Yale journal of biology and medicine · 2012Article
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Authors and funding
7 authors at 3 institutions in 1 country.
Funding
Abstract
Anthrax toxin is an A/B bacterial protein toxin which is composed of the enzymatically active Lethal Factor (LF) and/or Oedema Factor (EF) bound to Protective Antigen 63 (PA63) which functions as both the receptor binding and transmembrane domains. Once the toxin binds to its cell surface receptors it is internalized into the cell and traffics through Rab5- and Rab7-associated endosomal vesicles. Following acidification of the vesicle lumen, PA63 undergoes a dynamic change forming a beta-barrel that inserts into and forms a pore through the endosomal membrane. It is widely recognized that LF, and the related fusion protein LFnDTA, must be completely denatured in order to transit through the PA63 formed pore and enter the eukaryotic cell cytosol. We demonstrate by protease protection assays that the molecular chaperone GRP78 mediates the unfolding of LFnDTA and LF at neutral pH and thereby converts these proteins from a trypsin resistant to sensitive conformation. We have used immunoelectron microscopy and gold-labelled antibodies to demonstrate that both GRP78 and GRP94 chaperones are present in the lumen of endosomal vesicles. Finally, we have used siRNA to demonstrate that knock-down of GRP78 results in the emergence of resistance to anthrax lethal toxin and oedema toxin action.
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