ArticlePLoS pathogens2026
Ultrapotent neutralization of Bacillus anthracis toxin by a human antibody via blockade of PA oligomerization.
Article in PLoS pathogens, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 1 paper.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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
1 citing paper in PubMed.
Corrections and comments
- Erratum issued
Authors and funding
10 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Anthrax lethal toxin is a key virulence factor of Bacillus anthracis. However, non-canonical epitopes of protective antigen (PA) and alternative neutralization mechanisms beyond receptor blockade or prevention of proteolytic cleavage remain underexplored. Here, we characterize a fully human monoclonal antibody, 22F1, with ultrapotent toxin neutralization in vitro (IC50 = 0.027 nM) and in vivo (molar ratio 1:7.5-15). Unlike known PA antibodies, 22F1 selectively binds the post-cleavage form PA63, not full-length PA83, due to shielding of the epitope by PA20. Cryo-EM reveals a novel conformational epitope spanning domains D1', D2, and D3. 22F1 does not block receptor engagement, PA proteolytic activation, or lethal factor binding. Instead, its epitope lies near the inter-protomer interface; binding of a single 22F1 Fab to any PA63 protomer exerts a dual steric hindrance effect, simultaneously preventing additional Fab binding to adjacent protomers and blocking PA63 oligomerization. This "single-hit" mechanism enables one antibody molecule to efficiently block prepore formation, achieving high potency. Our findings advance anthrax antitoxin research and provide a paradigm for targeting other proteins with similar activation-oligomerization-pore formation mechanisms.
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