ArticleThe Biochemical journal2005
Cecropin P1 and novel nematode cecropins: a bacteria-inducible antimicrobial peptide family in the nematode Ascaris suum.
Article in The Biochemical journal, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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Who cites it
26 citing papers in PubMed.
- Uncovering evolutionarily remote and highly potent antimicrobial peptides with protein language models.Nature biomedical engineering · 2026Article
- Development of New Antimicrobial Peptides by Directional Selection.Antibiotics (Basel, Switzerland) · 2025Article
- Parasite-microbiota interactions: a pathway to innovative interventions for Chagas disease, leishmaniasis, and ascariasis.Future microbiology · 2025Review
- Relationship between pediatric asthma and respiratory microbiota, intestinal microbiota: a narrative review.Frontiers in microbiology · 2025Review
- Hydrolysis of Antimicrobial Peptides by Extracellular Peptidases in Wastewater.Environmental science & technology · 2024Article
- Getting around the roundworms: Identifying knowledge gaps and research priorities for the ascarids.Advances in parasitology · 2024Article
- Exploring the antimicrobial peptidome of nematodes through phylum-spanning in silico analyses highlights novel opportunities for pathogen control.PLoS neglected tropical diseases · 2023Article
- Novel integrated computational AMP discovery approaches highlight diversity in the helminth AMP repertoire.PLoS pathogens · 2023Article
- Antimicrobial Resistance and Recent Alternatives to Antibiotics for the Control of Bacterial Pathogens with an Emphasis on Foodborne Pathogens.Antibiotics (Basel, Switzerland) · 2023Review
- Helminths and Bacterial Microbiota: The Interactions of Two of Humans' "Old Friends".International journal of molecular sciences · 2022Review
- Three-Dimensional Structure of the Antimicrobial Peptide Cecropin P1 in Dodecylphosphocholine Micelles and the Role of the C-Terminal Residues.ACS omega · 2022Article
- Detangling the Crosstalk BetweenFrontiers in cellular and infection microbiology · 2022Review
- Article
- Antimicrobial Peptides: Novel Source and Biological Function With a Special Focus on Entomopathogenic Nematode/Bacterium Symbiotic Complex.Frontiers in microbiology · 2021Review
- Worms' Antimicrobial Peptides.Marine drugs · 2019Review
- Insect Antimicrobial Peptides, a Mini Review.Toxins · 2018Review
- Parasitic Nematodes Exert Antimicrobial Activity and Benefit From Microbiota-Driven Support for Host Immune Regulation.Frontiers in immunology · 2018Article
- The Intestinal RoundwormFrontiers in cellular and infection microbiology · 2018Article
- Reciprocal Interactions between Nematodes and Their Microbial Environments.Frontiers in cellular and infection microbiology · 2017Review
- Bactericide, Immunomodulating, and Wound Healing Properties of TransgenicJournal of immunology research · 2017Article
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Authors and funding
5 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Cecropin P1 was first identified as a mammalian antimicrobial peptide isolated from the pig intestine. Much research aimed at characterizing this peptide has been reported. Recently, the workers who discovered the peptide corrected their original conclusion, and confirmed that this peptide originates in fact from the pig intestinal parasitic nematode, Ascaris suum. In the present study, we carried out a semi-exhaustive search for bacteria-inducible transcripts in A. suum by the cDNA subtraction method. The transcripts encoding cecropin P1 and novel Ascaris cecropins, designated cecropins P2, P3 and P4, were found to be positively induced factors. Chemically synthesized Ascaris cecropins were bactericidal against a wide range of microbes, i.e. Gram-positive (Staphylococcus aureus, Bacillus subtilis and Micrococcus luteus) and Gram-negative (Pseudomonas aeruginosa, Salmonella typhimurium, Serratia marcescens and Esherichia coli) bacteria, and were weakly but detectably active against yeasts (Saccharomyces cerevisiae and Candida albicans). Cecropin P1-like sequences were also detected at least in two other species (Ascaris lumbricoides and Toxocara canis) of the Ascarididae. All Ascaris cecropin precursors contain an acidic pro-region connected by a tetra-basic cleavage site at the C-terminus. Such an acidic pro-region is also reported to be present in the tunicate cecropin-type antimicrobial peptide styelin. On the basis of the evolutionary position of nematodes and tunicates, the ancestral cecropin may have contained the acidic pro-region at the C-terminus.
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