Effect of antimicrobial peptides derived from human cathelicidin LL-37 on Entamoeba histolytica trophozoites
| Autor: | Eva E. Avila, Rosa Rico-Mata, Luis M. De León-Rodríguez |
|---|---|
| Rok vydání: | 2013 |
| Předmět: |
Erythrocytes
Gram-negative bacteria medicine.medical_treatment Immunology Antimicrobial peptides Antiprotozoal Agents Peptide Hemolysis Cathelicidin Microbiology Entamoeba histolytica Cathelicidins Cysteine Proteases medicine Humans Trophozoites chemistry.chemical_classification biology Entamoeba General Medicine biology.organism_classification Antimicrobial Peptide Fragments Amino acid Infectious Diseases chemistry Biochemistry Parasitology Antimicrobial Cationic Peptides |
| Zdroj: | Experimental Parasitology. 133:300-306 |
| ISSN: | 0014-4894 |
| DOI: | 10.1016/j.exppara.2012.12.009 |
| Popis: | The human cathelicidin hCAP18/LL-37 is an antimicrobial protein consisting of a conserved N-terminal prosequence called the cathelin-like domain and a C-terminal peptide called LL-37. This peptide contains 37 amino acid residues, and several truncated variants obtained from natural sources or by chemical synthesis differ in their capability to damage Gram positive and Gram negative bacteria as well as Candida albicans. KR-12 is the shortest peptide (12 amino acids) of LL-37 that has conserved antibacterial activity. In addition to LL-37, other active cathelicidin-derived peptides have been reported; for instance, the peptides KR-20, a 20-aa derivative of LL-37, and KS-30, a 30-aa derivative of LL-37, have been found in human sweat. Both peptides exhibit an overall increased antibacterial and antifungal activity when compared with LL-37. We investigated the effect of LL-37 and three peptides derived from this antimicrobial molecule, KR-12, KR-20 and KS-30, on the integrity of Entamoeba histolytica trophozoites. The four peptides showed effects on E. histolytica integrity and viability in the concentration range of 10–50 μM. The peptides KR-12, KR-20, KS-30 and LL-37 differed in their capability to damage the parasite integrity, with KR-20 being the most effective and with KR-12 and LL-37 being less active. These results demonstrate the ability of antimicrobial peptides derived from human cathelicidin to damage Entamoeba trophozoites. Moreover, it was shown that the integrity of the peptides is altered in the presence of an ameba soluble fraction with cysteine protease activity. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|
Full Text from ScienceDirect