ArticleThe Biochemical journal2006
Human alpha-defensins neutralize toxins of the mono-ADP-ribosyltransferase family.
Article in The Biochemical journal, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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Who cites it
25 citing papers in PubMed, 49 citations in OpenAlex.
- Novel endogenous protein-based strategies to inhibit clinically relevant bacterial AB-type toxins including pertussis toxin.Archives of toxicology · 2026Review
- A host defense role for Fibrinogen by direct binding of Clostridium botulinum C2 toxin.Cellular and molecular life sciences : CMLS · 2026Article
- The Battle Against Pertussis: Discovery of Endogenous Human Proteins and Peptides as Toxin-Inhibitors.Toxins · 2026Review
- Effects of Bile on PathogenicBiomolecules · 2025Article
- Promotion of Colitis in B Cell-Deficient C57BL/6 Mice Infected with EnterotoxigenicInternational journal of molecular sciences · 2023Article
- Inhibition of Pertussis Toxin by Human α-Defensins-1 and -5: Differential Mechanisms of Action.International journal of molecular sciences · 2023Article
- Article
- Synthesis of an Anti-CD7 Recombinant Immunotoxin Based on PE24 in CHO andInternational journal of molecular sciences · 2022Article
- Human α-Defensin-6 NeutralizesInternational journal of molecular sciences · 2022Article
- Review
- Article
- Human α-Defensin-5 Efficiently NeutralizesFrontiers in pharmacology · 2020Article
- A Simplified Derivative of Human Defensin 5 with Potent and Efficient Activity against Multidrug-Resistant Acinetobacter baumannii.Antimicrobial agents and chemotherapy · 2018Article
- 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
- Retrocyclins neutralize bacterial toxins by potentiating their unfolding.The Biochemical journal · 2015Article
- Human defensins facilitate local unfolding of thermodynamically unstable regions of bacterial protein toxins.Immunity · 2014Article
- Rattusin, an intestinal α-defensin-related peptide in rats with a unique cysteine spacing pattern and salt-insensitive antibacterial activities.Antimicrobial agents and chemotherapy · 2013Article
- Functional determinants of human enteric α-defensin HD5: crucial role for hydrophobicity at dimer interface.The Journal of biological chemistry · 2012Article
- Arginine-specific mono ADP-ribosylation in vitro of antimicrobial peptides by ADP-ribosylating toxins.PloS one · 2012Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Various bacterial pathogens secrete toxins, which are not only responsible for fatal pathogenesis of disease, but also facilitate evasion of host defences. One of the best-known bacterial toxin groups is the mono-ADP-ribosyltransferase family. In the present study, we demonstrate that human neutrophil alpha-defensins are potent inhibitors of the bacterial enzymes, particularly against DT (diphtheria toxin) and ETA (Pseudomonas exotoxin A). HNP1 (human neutrophil protein 1) inhibited DT- or ETA-mediated ADP-ribosylation of eEF2 (eukaryotic elongation factor 2) and protected HeLa cells against DT- or ETA-induced cell death. Kinetic analysis revealed that inhibition of DT and ETA by HNP1 was competitive with respect to eEF2 and uncompetitive against NAD+ substrates. Our results reveal that toxin neutralization represents a novel biological function of HNPs in host defence.
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