July 25, 2025Open Access

Widespread repurposing of the human CD38 ADP-ribosyl cyclase fold for toxicity in antibacterial and anti-eukaryotic bacterial polymorphic toxins

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Discussion

Novel bacterial toxin exhibits CD38-like function and NAD+ hydrolysis, suggesting new microbial warfare strategies.

The study identifies a unique toxin in Pantoea ananatis that resembles the human CD38 enzyme.
Functional assays show that ADP-ribosyl cyclase domains act as potent NAD-depleting toxins.
Comparative genomics indicate widespread distribution of CD38-like domains in various bacterial systems.
These findings enhance our understanding of microbial toxins and their interactions with host cells.

Martinkus et al. (2025) studied this question.

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