ArticleAntimicrobial agents and chemotherapy2011
Recombinant anthrax toxin receptor-Fc fusion proteins produced in plants protect rabbits against inhalational anthrax.
Article in Antimicrobial agents and chemotherapy, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed, 44 citations in OpenAlex.
- Effect of plant produced Anti-hIL-6 receptor antibody blockade on pSTAT3 expression in human peripheral blood mononuclear cells.Scientific reports · 2023Article
- Prevention of Shiga toxin 1-caused colon injury by plant-derived recombinant IgA.Scientific reports · 2022Article
- Capillary morphogenesis gene 2 (CMG2) mediates growth factor-induced angiogenesis by regulating endothelial cell chemotaxis.Angiogenesis · 2022Article
- An optimized Factor H-Fc fusion protein against multidrug-resistantFrontiers in immunology · 2022Article
- Article
- Development of Complement Factor H-Based Immunotherapeutic Molecules in Tobacco Plants Against Multidrug-ResistantFrontiers in immunology · 2020Article
- Inhibition of Pore-Forming Proteins.Toxins · 2019Review
- Effects of N-Glycosylation on the Structure, Function, and Stability of a Plant-Made Fc-Fusion Anthrax Decoy Protein.Frontiers in plant science · 2019Article
- Transient Recombinant Protein Production in GlycoengineeredInternational journal of molecular sciences · 2018Article
- Glycoform Modification of Secreted Recombinant Glycoproteins through Kifunensine Addition during Transient Vacuum Agroinfiltration.International journal of molecular sciences · 2018Article
- Hydroponic Treatment ofFrontiers in plant science · 2018Article
- Protection of Human Colon Cells from Shiga Toxin by Plant-based Recombinant Secretory IgA.Scientific reports · 2017Article
- Expression, Purification, and Biophysical Characterization of a Secreted Anthrax Decoy Fusion Protein in Nicotiana benthamiana.International journal of molecular sciences · 2017Article
- Roles of Anthrax Toxin Receptor 2 in Anthrax Toxin Membrane Insertion and Pore Formation.Toxins · 2016Review
- Article
- Anti-infective immunoadhesins from plants.Plant biotechnology journal · 2015Review
- An overview of investigational toxin-directed therapies for the adjunctive management of Bacillus anthracis infection and sepsis.Expert opinion on investigational drugs · 2015Review
- Anthrax lethal and edema toxins in anthrax pathogenesis.Trends in microbiology · 2014Review
- Improving the anti-toxin abilities of the CMG2-Fc fusion protein with the aid of computational design.PloS one · 2014Article
- Delayed toxicity associated with soluble anthrax toxin receptor decoy-Ig fusion protein treatment.PloS one · 2012Article
Corrections and comments
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Authors and funding
12 authors at 5 institutions in 1 country.
Funding
Abstract
Inhalational anthrax, a zoonotic disease caused by the inhalation of Bacillus anthracis spores, has a ∼50% fatality rate even when treated with antibiotics. Pathogenesis is dependent on the activity of two toxic noncovalent complexes: edema toxin (EdTx) and lethal toxin (LeTx). Protective antigen (PA), an essential component of both complexes, binds with high affinity to the major receptor mediating the lethality of anthrax toxin in vivo, capillary morphogenesis protein 2 (CMG2). Certain antibodies against PA have been shown to protect against anthrax in vivo. As an alternative to anti-PA antibodies, we produced a fusion of the extracellular domain of human CMG2 and human IgG Fc, using both transient and stable tobacco plant expression systems. Optimized expression led to the CMG2-Fc fusion protein being produced at high levels: 730 mg/kg fresh leaf weight in Nicotiana benthamiana and 65 mg/kg in N. tabacum. CMG2-Fc, purified from tobacco plants, fully protected rabbits against a lethal challenge with B. anthracis spores at a dose of 2 mg/kg body weight administered at the time of challenge. Treatment with CMG2-Fc did not interfere with the development of the animals' own immunity to anthrax, as treated animals that survived an initial challenge also survived a rechallenge 30 days later. The glycosylation of the Fc (or lack thereof) had no significant effect on the protective potency of CMG2-Fc in rabbits or on its serum half-life, which was about 5 days. Significantly, CMG2-Fc effectively neutralized, in vitro, LeTx-containing mutant forms of PA that were not neutralized by anti-PA monoclonal antibodies.
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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.