Identification, Characterization, Immunolocalization, and Biological Activity of Lucilin Peptide
| Autor: | Jhon Carlos Castaño, Lily Johana Toro, Germán Alberto Téllez, Jesica Alejandra Zapata, Juan Valentin Trujillo, Juan David Rivera, Juan Pablo Bedoya, Bruno Rivas-Santiago, Richard Onalbi Hoyos, Diana Carolina Henao |
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| Rok vydání: | 2018 |
| Předmět: |
0301 basic medicine
Gram-negative bacteria Veterinary (miscellaneous) 030106 microbiology Peptide Hemolysis Microbiology 03 medical and health sciences Staphylococcus epidermidis Hemolymph Animals Humans chemistry.chemical_classification Peptide analog biology Tumor Necrosis Factor-alpha fungi Cecropins Biological activity Antimicrobial biology.organism_classification 030104 developmental biology Infectious Diseases Cecropin chemistry Insect Science Pseudomonas aeruginosa Leukocytes Mononuclear Parasitology |
| Zdroj: | Acta tropica. 185 |
| ISSN: | 1873-6254 |
| Popis: | Maggots from the Lucilia sp. genus are used for debridement of infected and necrotic wounds. Broad-spectrum antimicrobial activity has been described in the excretion/secretions (ES 1 ) of these larvae. This study identifies the genetic sequence of a cecropin-like antimicrobial peptide from Lucilia eximia. Total RNA was extracted and used for PCR-RACE amplification of a cecropin, the native peptide was immunolocalized in the tissues and secretions of the larvae, and a synthetic analog was used to explore its antimicrobial, cytotoxic, LPS neutralizing and wound-healing activities in vitro. The genetic cDNA sequence of a cecropin-like antimicrobial peptide in L. eximia called “Lucilin” was amplified, corresponding to 63 aa completed protein and 40 aa mature peptide; the structure of the mature peptide was predicted as an α-helix. The peptide was immunolocalized in the salivary glands, fat body, the ES, and hemolymph of the maggots. Lucilin synthetic peptide analog was active against E. coli DH10B with a MIC 2 of 7.8 μg/mL, E. coli extended spectrum b-lactamase (ESBL) (MIC: 15.6 μg/mL), and Enterobacter cloacae (MIC: 125 μg/mL), but it was not active against Pseudomonas aeruginosa and Staphylococcus epidermidis; and had no cytotoxic or hemolytic activity. It showed immunomodulatory activity against human peripheral blood mononuclear cells (PBMCs) stimulated with LPS, reducing the TNF-α production when treated at 17 μg/mL and induces cell migration of Hacat at 5 and 50 μg/mL. Lucilin is a cecropin-like peptide from L. eximia with antimicrobial activity against Gram negative bacteria and immunomodulatory activities, decreasing the TNF-α production in PBMCs and inducing cellular migration in human keratinocytes. |
| Databáze: | OpenAIRE |
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