ArticleInfection and immunity2009
Novel chimpanzee/human monoclonal antibodies that neutralize anthrax lethal factor, and evidence for possible synergy with anti-protective antigen antibody.
Article in Infection and immunity, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.
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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
32 citing papers in PubMed, 52 citations in OpenAlex.
- Ultrapotent neutralization of Bacillus anthracis toxin by a human antibody via blockade of PA oligomerization.PLoS pathogens · 2026Article
- Bispecific antibody engineered from two non-protective antibodies confers full protection against anthrax toxin through inhibition of PA83 cleavage.Microbiology spectrum · 2025Article
- Characterization of the UK anthrax vaccine and human immunogenicity.Human vaccines & immunotherapeutics · 2021Article
- Human monoclonal anti-protective antigen antibody for the low-dose post-exposure prophylaxis and treatment of Anthrax.BMC infectious diseases · 2018Article
- Lethal factor antibodies contribute to lethal toxin neutralization in recipients of anthrax vaccine precipitated.Vaccine · 2017Article
- Monoclonal Antibodies and Antibody Like Fragments Derived from Immunised Phage Display Libraries.Advances in experimental medicine and biology · 2017Review
- A Diverse Set of Single-domain Antibodies (VHHs) against the Anthrax Toxin Lethal and Edema Factors Provides a Basis for Construction of a Bispecific Agent That Protects against Anthrax Infection.The Journal of biological chemistry · 2016Article
- A Novel Chimeric Anti-PA Neutralizing Antibody for Postexposure Prophylaxis and Treatment of Anthrax.Scientific reports · 2015Article
- Review
- A heterodimer of a VHH (variable domains of camelid heavy chain-only) antibody that inhibits anthrax toxin cell binding linked to a VHH antibody that blocks oligomer formation is highly protective in an anthrax spore challenge model.The Journal of biological chemistry · 2015Article
- Back to the future: recombinant polyclonal antibody therapeutics.Current opinion in chemical engineering · 2013Article
- Development of Norwalk virus-specific monoclonal antibodies with therapeutic potential for the treatment of Norwalk virus gastroenteritis.Journal of virology · 2013Article
- Combinations of monoclonal antibodies to anthrax toxin manifest new properties in neutralization assays.Infection and immunity · 2013Article
- Disease-enhancing antibodies improve the efficacy of bacterial toxin-neutralizing antibodies.Cell host & microbe · 2013Article
- A comparison of binding surfaces for SPR biosensing using an antibody-antigen system and affinity distribution analysis.Methods (San Diego, Calif.) · 2013Article
- Article
- A human/murine chimeric fab antibody neutralizes anthrax lethal toxin in vitro.Clinical & developmental immunology · 2013Article
- Article
- Engineered domain-based assays to identify individual antibodies in oligoclonal combinations targeting the same protein.Analytical biochemistry · 2012Article
- An overview of anthrax infection including the recently identified form of disease in injection drug users.Intensive care medicine · 2012Review
Corrections and comments
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Authors and funding
8 authors at 2 institutions in 1 country.
Funding
Abstract
Three chimpanzee Fabs reactive with lethal factor (LF) of anthrax toxin were isolated and converted into complete monoclonal antibodies (MAbs) with human gamma1 heavy-chain constant regions. In a macrophage toxicity assay, two of the MAbs, LF10E and LF11H, neutralized lethal toxin (LT), a complex of LF and anthrax protective antigen (PA). LF10E has the highest reported affinity for a neutralizing MAb against LF (dissociation constant of 0.69 nM). This antibody also efficiently neutralized LT in vitro, with a 50% effective concentration (EC(50)) of 0.1 nM, and provided 100% protection of rats against toxin challenge with a 0.5 submolar ratio relative to LT. LF11H, on the other hand, had a slightly lower binding affinity to LF (dissociation constant of 7.4 nM) and poor neutralization of LT in vitro (EC(50) of 400 nM) and offered complete protection in vivo only at an equimolar or higher ratio to toxin. Despite this, LF11H, but not LF10E, provided robust synergistic protection when combined with MAb W1, which neutralizes PA. Epitope mapping and binding assays indicated that both LF10E and LF11H recognize domain I of LF (amino acids 1 to 254). Although domain I is responsible for binding to PA, neither MAb prevented LF from binding to activated PA. Although two unique MAbs could protect against anthrax when used alone, even more efficient and broader protection should be gained by combining them with anti-PA MAbs.
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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.