ArticleCellular and molecular life sciences : CMLS2026
A host defense role for Fibrinogen by direct binding of Clostridium botulinum C2 toxin.
Article in Cellular and molecular life sciences : CMLS, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
0 citing papers in PubMed.
No citing paper in PubMed yet.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
8 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In addition to fibrinogens canonical function in hemostasis, alternate roles in innate immunity have emerged. However, interactions with bacterial protein toxins, the main virulence factors of many medically relevant bacteria and causative agents of life-threatening diseases, have not been described so far. Here, we identified human fibrinogen as an inhibitor of the enterotoxic Clostridium (C.) botulinum C2 toxin. Our results indicate that fibrinogen specifically interacts with the binding subunit of C2 toxin in vitro and that N-linked glycans of fibrinogen are crucial for this interaction. This prevents receptor-binding and cellular uptake of the toxin. Related toxins from Bacillus anthracis (lethal toxin), C. perfringens (iota) or Clostridioides difficile (CDT) do not bind to fibrinogen and are therefore not inhibited. Furthermore, C2 toxin had no effect on coagulation of human blood ex vivo. In conclusion, we identified fibrinogen as an inhibitor of a highly potent bacterial protein toxin, highlighting an unexpected role for this blood coagulation factor in innate immunity.
Indexed as
Identifiers
What OpenQuestion holds
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.