ArticlePloS one2012
Arginine-specific mono ADP-ribosylation in vitro of antimicrobial peptides by ADP-ribosylating toxins.
Article in PloS one, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 22 citations in OpenAlex.
- HNP-1: From Structure to Application Thanks to Multifaceted Functions.Microorganisms · 2025Review
- Inhibition of Pertussis Toxin by Human α-Defensins-1 and -5: Differential Mechanisms of Action.International journal of molecular sciences · 2023Article
- Mono-ADP-ribosylation sites of human CD73 inhibit its adenosine-generating enzymatic activity.Purinergic signalling · 2022Article
- Community-Acquired Respiratory Distress Syndrome Toxin: Unique Exotoxin forFrontiers in microbiology · 2021Review
- MAV_4644 Interaction with the Host Cathepsin Z ProtectsMicroorganisms · 2019Article
- Targeting and inactivation of bacterial toxins by human defensins.Biological chemistry · 2017Review
- The NarE protein of Neisseria gonorrhoeae catalyzes ADP-ribosylation of several ADP-ribose acceptors despite an N-terminal deletion.FEMS microbiology letters · 2016Article
- ADP-Ribosylargininyl reaction of cholix toxin is mediated through diffusible intermediates.BMC biochemistry · 2014Article
- Human defensins facilitate local unfolding of thermodynamically unstable regions of bacterial protein toxins.Immunity · 2014Article
- In vitro assays to monitor the activity of Pseudomonas aeruginosa Type III secreted proteins.Methods in molecular biology (Clifton, N.J.) · 2014Article
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Authors and funding
9 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Among the several toxins used by pathogenic bacteria to target eukaryotic host cells, proteins that exert ADP-ribosylation activity represent a large and studied family of dangerous and potentially lethal toxins. These proteins alter cell physiology catalyzing the transfer of the ADP-ribose unit from NAD to cellular proteins involved in key metabolic pathways. In the present study, we tested the capability of four of these toxins, to ADP-ribosylate α- and β- defensins. Cholera toxin (CT) from Vibrio cholerae and heat labile enterotoxin (LT) from Escherichia coli both modified the human α-defensin (HNP-1) and β- defensin-1 (HBD1), as efficiently as the mammalian mono-ADP-ribosyltransferase-1. Pseudomonas aeruginosa exoenzyme S was inactive on both HNP-1 and HBD1. Neisseria meningitidis NarE poorly recognized HNP-1 as a substrate but it was completely inactive on HBD1. On the other hand, HNP-1 strongly influenced NarE inhibiting its transferase activity while enhancing auto-ADP-ribosylation. We conclude that only some arginine-specific ADP-ribosylating toxins recognize defensins as substrates in vitro. Modifications that alter the biological activities of antimicrobial peptides may be relevant for the innate immune response. In particular, ADP-ribosylation of antimicrobial peptides may represent a novel escape mechanism adopted by pathogens to facilitate colonization of host tissues.
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