ArticleInfection and immunity2001
Purification of anthrax edema factor from Escherichia coli and identification of residues required for binding to anthrax protective antigen.
Article in Infection and immunity, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 39 citations in OpenAlex.
- Early Circulating Edema Factor in Inhalational Anthrax Infection: Does It Matter?Microorganisms · 2024Article
- Anthrax revisited: how assessing the unpredictable can improve biosecurity.Frontiers in bioengineering and biotechnology · 2023Article
- Molecular and Genomic Characterization of PFAB2: A Non-virulentCurrent genomics · 2019Article
- Review
- A chimeric protein that functions as both an anthrax dual-target antitoxin and a trivalent vaccine.Antimicrobial agents and chemotherapy · 2010Article
- Residue histidine 669 is essential for the catalytic activity of Bacillus anthracis lethal factor.Journal of bacteriology · 2010Article
- The major neutralizing antibody responses to recombinant anthrax lethal and edema factors are directed to non-cross-reactive epitopes.Infection and immunity · 2009Article
- Bacillus anthracis edema toxin impairs neutrophil actin-based motility.Infection and immunity · 2009Article
- Lethal and edema toxins in the pathogenesis of Bacillus anthracis septic shock: implications for therapy.American journal of respiratory and critical care medicine · 2007Review
- Binary bacterial toxins: biochemistry, biology, and applications of common Clostridium and Bacillus proteins.Microbiology and molecular biology reviews : MMBR · 2004Review
- Anthrax edema toxin requires influx of calcium for inducing cyclic AMP toxicity in target cells.Infection and immunity · 2002Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The structural gene for anthrax edema factor (EF) was expressed in Escherichia coli under the control of a powerful T5 promoter to yield the 89-kDa recombinant protein that reacted with anti-EF antibodies. Recombinant EF was purified to homogeneity by a two-step procedure involving metal chelate affinity chromatography and cation-exchange chromatography. From 1 liter of culture, 2.5 mg of biologically active EF was easily purified. This is the first report of purification of anthrax EF from E. coli. EF purified from E. coli was biologically and functionally as active as its Bacillus anthracis counterpart. The recombinant protein could compete with lethal factor for binding to protective antigen. Sequence analysis revealed a stretch of seven amino acids, Val Tyr Tyr Glu Ile Gly Lys, present both in EF (residues 136 to 142) and lethal factor (residues 147 to 153). To investigate the role of these seven residues in binding to protective antigen, the residues were individually mutated to alanine in EF. Mutations in residues Tyr137, Tyr138, Ile140, and Lys142 of EF specifically blocked its interaction with anthrax protective antigen. The adenylate cyclase activity of the mutants remained unaffected. The results suggested that residues Tyr137, Tyr138, Ile140, and Lys142 are required for binding of EF to anthrax protective antigen, which facilitates its entry into susceptible cells.
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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.