What question did this study set out to answer?

Identify and characterize a novel polymorphic toxin domain in Pantoea ananatis and determine its structural, functional, and evolutionary relationship to human CD38.

September 27, 2025Journal of Biological ChemistryOpen Access

Widespread deployment of the human CD38 ADP-ribosyl cyclase fold in antibacterial and anti-eukaryotic polymorphic toxins

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Authors

JMJulius MartinkusCentre National de la Recherche Scientifique LTLaurent TerradotUniversité Claude Bernard Lyon 1 DJDukas JurėnasUniversité Libre de Bruxelles

Discussion

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Implication

Structural and biochemical analysis reveals CD38-like ADP-ribosyl cyclase toxin domains in bacteria, indicating widespread co-option of human-like metabolic enzymes for intermicrobial warfare.

Key Points

Identify and characterize a novel polymorphic toxin domain in Pantoea ananatis and determine its structural, functional, and evolutionary relationship to human CD38.
Determined the 1.6-Å resolution crystal structure of the C-terminal ADP-ribosyl cyclase (ARC) domain from Pantoea ananatis.
Assayed in vitro and in vivo enzymatic hydrolysis of NAD+ and NADP+ alongside growth inhibition experiments in bacterial and eukaryotic cells.
Performed comparative genomics across bacterial secretion systems (T6SS, T7SS, and CDI) and tested cross-immunity between non-cognate toxin–immunity pairs.
The 1.6-Å crystal structure revealed that the bacterial ARC domain adopts a globular fold nearly identical to human CD38 ADP-ribosyl cyclase with conserved catalytic residues.
Toxin activity caused rapid depletion of NAD+ and NADP+ in vitro and in vivo, leading to potent growth inhibition across both bacterial and eukaryotic cells.
Genomic profiling demonstrated that CD38-like ARC domains are widely distributed across diverse bacterial delivery modules, showing functional cross-immunity between non-cognate pairs.

Cite This Study

Martinkus et al. (2025) studied this question.

synapsesocial.com/papers/6a7253a875498292b70b7611 https://doi.org/10.1016/j.jbc.2025.110775

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Implication

Structural and biochemical analysis reveals CD38-like ADP-ribosyl cyclase toxin domains in bacteria, indicating widespread co-option of human-like metabolic enzymes for intermicrobial warfare.

Widespread deployment of the human CD38 ADP-ribosyl cyclase fold in antibacterial and anti-eukaryotic polymorphic toxins

Discussion

Member takes

Implication

Key Points

Cite This Study

Widespread deployment of the human CD38 ADP-ribosyl cyclase fold in antibacterial and anti-eukaryotic polymorphic toxins

Discussion

Member takes

Implication

Key Points

Cite This Study

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