ArticleScientific reports2019
Cathelicidins PMAP-36, LL-37 and CATH-2 are similar peptides with different modes of action.
Article in Scientific reports, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 49 papers.
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Who cites it
49 citing papers in PubMed, 100 citations in OpenAlex.
- Chicken cathelicidin-3 protected mice from avian pathogenic Escherichia coli infection mediated by triggering chemokine CCL3 pathway.Veterinary research · 2026Article
- Aggregation-State Dynamics Drive Double Cooperativity Between Antimicrobial Peptides LL-37 and HNP1.Angewandte Chemie (International ed. in English) · 2026Article
- Peptides as a Therapeutic Alternative Against Leishmaniasis: A Scoping Review.Chemical biology & drug design · 2026Article
- Bacterial cell fate under stress: lipid remodeling and antimicrobial peptide attack.npj antimicrobials and resistance · 2026Article
- A hedgehog cathelicidin-derived peptide exhibits antiviral activity against herpes simplex virus type 1 infection.Frontiers in microbiology · 2026Article
- Identification and characterization of novel antimicrobial peptides fromFrontiers in immunology · 2026Article
- Integrated Transcriptomic and Metabolomic Analysis Reveals Regulatory Effects of Fermented Chinese Chive on Early Testicular Development in Piglets.Antioxidants (Basel, Switzerland) · 2025Article
- Testing antimicrobial peptides inhibiting protein synthesis in livingFrontiers in microbiology · 2025Article
- Cathelicidin: Insights into Its Impact on Metabolic Syndrome and Chronic Inflammation.Metabolites · 2024Review
- Recombinant Lactococcus lactis Expressing Human LL-37 Prevents Deaths from Viral Infections in Piglets and Chicken.Probiotics and antimicrobial proteins · 2024Article
- Antimicrobial Peptide CATH-2 Attenuates Avian PathogenicInternational journal of molecular sciences · 2024Article
- Immunomodulatory properties of chicken cathelicidin-2 investigated on an ileal explant culture.Veterinary research communications · 2024Article
- Antibacterial activity of the antimicrobial peptide PMAP-36 in combination with tetracycline against porcine extraintestinal pathogenic Escherichia coli in vitro and in vivo.Veterinary research · 2024Article
- CATH-2-derived antimicrobial peptide inhibits multidrug-resistantFrontiers in cellular and infection microbiology · 2024Article
- Structure, Function, and Physicochemical Properties of Pore-forming Antimicrobial Peptides.Current pharmaceutical biotechnology · 2024Review
- Effects ofPharmaceuticals (Basel, Switzerland) · 2023Article
- Structural and biological characterization of shortened derivatives of the cathelicidin PMAP-36.Scientific reports · 2023Article
- A wild boar cathelicidin peptide derivative inhibits severe acute respiratory syndrome coronavirus-2 and its drifted variants.Scientific reports · 2023Article
- Cell unit-inspired natural nano-based biomaterials as versatile building blocks for bone/cartilage regeneration.Journal of nanobiotechnology · 2023Review
- The protective role of chicken cathelicidin-1 against Streptococcus suis serotype 2 in vitro and in vivo.Veterinary research · 2023Article
Corrections and comments
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Authors and funding
8 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Host defense peptides (HDPs) play a pivotal role in innate immunity and have, in addition to antimicrobial activity, also important immunomodulatory functions. Bacteria are less likely to develop resistance against HDPs because these peptides target and kill bacteria in multiple ways, as well as modulate the immune system. Therefore, HDPs, and derivatives thereof, are promising alternatives to traditional antibiotics. Hardly anything is known about the immunomodulatory functions of porcine cathelicidin PMAP-36. In this study, we aimed to determine both antibacterial and immunomodulatory activities of PMAP-36 comparing the properties of PMAP-36 analogs with two well-studied peptides, human LL-37 and chicken CATH-2. Transmission electron microscopy revealed different killing mechanisms of E. coli for PMAP-36, CATH-2 and LL-37. LL-37 binds LPS very weakly in contrast to PMAP-36, but it inhibits LPS activation of macrophages the strongest. The first 11 amino acids of the N-terminal side of PMAP-36 are dispensable for E. coli killing, LPS-neutralization and binding. Deletion of four additional amino acids resulted in a strong decrease in activity. The activity of full length PMAP-36 was not affected by monomerization, whereas the shorter analogs require dimerization for proper immunomodulatory activity but not for their antibacterial activity.
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