ArticleAntimicrobial agents and chemotherapy2012
Antimicrobial action and cell agglutination by the eosinophil cationic protein are modulated by the cell wall lipopolysaccharide structure.
Article in Antimicrobial agents and chemotherapy, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.
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Who cites it
37 citing papers in PubMed.
- Article
- Total Chemical Synthesis and Evaluation of the Antimicrobial Properties of Porcine β-Defensin 5 Against Gram-Positive and Gram-Negative Bacteria.Probiotics and antimicrobial proteins · 2026Article
- The antimicrobial peptide EM86 loaded to gamma-irradiated sodium alginate/polyvinyl alcohol electrospun nanofibrous dressing treated multidrug-resistantFrontiers in bioengineering and biotechnology · 2026Article
- Investigation on the Synergy between Membrane Permeabilizing Amphiphilic α-Hydrazido Acids and Commonly Used Antibiotics against Drug-Resistant Bacteria.Molecules (Basel, Switzerland) · 2024Article
- Ribonuclease 4 functions as an intestinal antimicrobial protein to maintain gut microbiota and metabolite homeostasis.Nature communications · 2024Article
- A Common Polymorphism inInternational journal of molecular sciences · 2024Article
- Molecular characterization, expression pattern and immunologic function ofFrontiers in immunology · 2024Article
- Synergistic Effect, Improved Cell Selectivity, and Elucidating the Action Mechanism of Antimicrobial Peptide YS12.International journal of molecular sciences · 2023Article
- Conformational exchange divergence along the evolutionary pathway of eosinophil-associated ribonucleases.Structure (London, England : 1993) · 2023Article
- Amyloid peptides with antimicrobial and/or microbial agglutination activity.Applied microbiology and biotechnology · 2022Review
- The Importance of 6-Aminohexanoic Acid as a Hydrophobic, Flexible Structural Element.International journal of molecular sciences · 2021Review
- Antibacterial effects assessment on some livestock pathogens, thermal stability and proposing a probable reason for different levels of activity of thanatin.Scientific reports · 2021Article
- The broad-spectrum antibiofilm activity of amyloid-forming hexapeptides.Microbial biotechnology · 2021Article
- Comparison of urine proteome among rat models by intraperitoneal injection with single bacteria and co-injection with two bacteria.PloS one · 2021Article
- Rapid Formation of Peptide/Lipid Coaggregates by the Amyloidogenic Seminal Peptide PAPBiophysical journal · 2020Article
- Design, Engineering and Discovery of Novel α-Helical and β-Boomerang Antimicrobial Peptides against Drug Resistant Bacteria.International journal of molecular sciences · 2020Review
- Thanatin Impairs Lipopolysaccharide Transport Complex Assembly by Targeting LptC-LptA Interaction and Decreasing LptA Stability.Frontiers in microbiology · 2020Article
- Antimicrobial Role of RNASET2 Protein During Innate Immune Response in the Medicinal LeechFrontiers in immunology · 2020Article
- Molecular anatomy of the receptor binding module of a bacteriophage long tail fiber.PLoS pathogens · 2019Article
- Insight into the Antifungal Mechanism of Action of Human RNase N-terminus Derived Peptides.International journal of molecular sciences · 2019Article
Corrections and comments
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Authors and funding
6 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Antimicrobial proteins and peptides (AMPs) are essential effectors of innate immunity, acting as a first line of defense against bacterial infections. Many AMPs exhibit high affinity for cell wall structures such as lipopolysaccharide (LPS), a potent endotoxin able to induce sepsis. Hence, understanding how AMPs can interact with and neutralize LPS endotoxin is of special relevance for human health. Eosinophil cationic protein (ECP) is an eosinophil secreted protein with high activity against both Gram-negative and Gram-positive bacteria. ECP has a remarkable affinity for LPS and a distinctive agglutinating activity. By using a battery of LPS-truncated E. coli mutant strains, we demonstrate that the polysaccharide moiety of LPS is essential for ECP-mediated bacterial agglutination, thereby modulating its antimicrobial action. The mechanism of action of ECP at the bacterial surface is drastically affected by the LPS structure and in particular by its polysaccharide moiety. We have also analyzed an N-terminal fragment that retains the whole protein activity and displays similar cell agglutination behavior. Conversely, a fragment with further minimization of the antimicrobial domain, though retaining the antimicrobial capacity, significantly loses its agglutinating activity, exhibiting a different mechanism of action which is not dependent on the LPS composition. The results highlight the correlation between the protein's antimicrobial activity and its ability to interact with the LPS outer layer and promote bacterial agglutination.
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