ArticleProceedings of the National Academy of Sciences of the United States of America2010
Anthrax toxin-neutralizing antibody reconfigures the protective antigen heptamer into a supercomplex.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
What it found
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The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
12 citing papers in PubMed.
- Human monoclonal anti-protective antigen antibody for the low-dose post-exposure prophylaxis and treatment of Anthrax.BMC infectious diseases · 2018Article
- Biochip for the Detection of Bacillus anthracis Lethal Factor and Therapeutic Agents against Anthrax Toxins.Membranes · 2016Article
- Review
- Article
- An important role of α-hemolysin in extracellular vesicles on the development of atopic dermatitis induced by Staphylococcus aureus.PloS one · 2014Article
- The sub-nanomolar binding of DNA-RNA hybrids by the single-chain Fv fragment of antibody S9.6.Journal of molecular recognition : JMR · 2013Article
- Disease-enhancing antibodies improve the efficacy of bacterial toxin-neutralizing antibodies.Cell host & microbe · 2013Article
- Antibody to ricin a chain hinders intracellular routing of toxin and protects cells even after toxin has been internalized.PloS one · 2013Article
- Obstructing toxin pathways by targeted pore blockage.Chemical reviews · 2012Review
- A three-dose intramuscular injection schedule of anthrax vaccine adsorbed generates sustained humoral and cellular immune responses to protective antigen and provides long-term protection against inhalation anthrax in rhesus macaques.Clinical and vaccine immunology : CVI · 2012Article
- Review
- Monoclonal antibody therapies against anthrax.Toxins · 2011Review
Corrections and comments
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Authors and funding
5 authors.
Funding
Abstract
The tripartite protein exotoxin secreted by Bacillus anthracis, a major contributor to its virulence and anthrax pathogenesis, consists of binary complexes of the protective antigen (PA) heptamer (PA63h), produced by proteolytic cleavage of PA, together with either lethal factor or edema factor. The mouse monoclonal anti-PA antibody 1G3 was previously shown to be a potent antidote that shares F(C) domain dependency with the human monoclonal antibody MDX-1303 currently under clinical development. Here we demonstrate that 1G3 instigates severe perturbation of the PA63h structure and creates a PA supercomplex as visualized by electron microscopy. This phenotype, produced by the unconventional mode of antibody action, highlights the feasibility for optimization of vaccines based on analogous structural modification of PA63h as an additional strategy for future remedies against anthrax.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.