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Antimicrobial and immunomodulatory activities of porcine cathelicidin Protegrin-1.
Javed, Ali; Oedairadjsingh, Trishana; Ludwig, Irene S; Wood, Thomas M; Martin, Nathaniel I; Broere, Femke; Weingarth, Markus H; Veldhuizen, Edwin J A.
Affiliation
  • Javed A; Faculty of Veterinary Medicine, Department of Biomolecular Health Sciences, Division Infectious Diseases & Immunology, Section Immunology, Utrecht University, the Netherlands; NMR Spectroscopy, Bijvoet Centre for Biomolecular Research, Department of Chemistry, Faculty of Science, Utrecht Univers
  • Oedairadjsingh T; Faculty of Veterinary Medicine, Department of Biomolecular Health Sciences, Division Infectious Diseases & Immunology, Section Immunology, Utrecht University, the Netherlands.
  • Ludwig IS; Faculty of Veterinary Medicine, Department of Biomolecular Health Sciences, Division Infectious Diseases & Immunology, Section Immunology, Utrecht University, the Netherlands.
  • Wood TM; Biological Chemistry Group, Institute of Biology Leiden, Leiden University, the Netherlands.
  • Martin NI; Biological Chemistry Group, Institute of Biology Leiden, Leiden University, the Netherlands.
  • Broere F; Faculty of Veterinary Medicine, Department of Biomolecular Health Sciences, Division Infectious Diseases & Immunology, Section Immunology, Utrecht University, the Netherlands.
  • Weingarth MH; NMR Spectroscopy, Bijvoet Centre for Biomolecular Research, Department of Chemistry, Faculty of Science, Utrecht University, the Netherlands.
  • Veldhuizen EJA; Faculty of Veterinary Medicine, Department of Biomolecular Health Sciences, Division Infectious Diseases & Immunology, Section Immunology, Utrecht University, the Netherlands. Electronic address: e.j.a.veldhuizen@uu.nl.
Mol Immunol ; 173: 100-109, 2024 Sep.
Article in En | MEDLINE | ID: mdl-39094445
ABSTRACT
Antimicrobial peptides (AMPs) are a promising alternative to antibiotics in the fight against multi-drug resistant and immune system-evading bacterial infections. Protegrins are porcine cathelicidins which have been identified in porcine leukocytes. Protegrin-1 is the best characterized family member and has broad antibacterial activity by interacting and permeabilizing bacterial membranes. Many host defense peptides (HDPs) like LL-37 or chicken cathelicidin 2 (CATH-2) have also been shown to have protective biological functions during infections. In this regard, it is interesting to study if Protegrin-1 has the immune modulating potential to suppress unnecessary immune activation by neutralizing endotoxins or by influencing the macrophage functionality in addition to its direct antimicrobial properties. This study showed that Protegrin-1 neutralized lipopolysaccharide- (LPS) and bacteria-induced activation of RAW macrophages by binding and preventing LPS from cell surface attachment. Furthermore, the peptide treatment not only inhibited bacterial phagocytosis by murine and porcine macrophages but also interfered with cell surface and intracellular bacterial survival. Lastly, Protegrin-1 pre-treatment was shown to inhibit the amastigote survival in Leishmania infected macrophages. These experiments describe an extended potential of Protegrin-1's protective role during microbial infections and add to the research towards clinical application of cationic AMPs.
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Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Phagocytosis / Lipopolysaccharides / Antimicrobial Cationic Peptides / Cathelicidins / Macrophages Limits: Animals Language: En Journal: Mol Immunol Year: 2024 Document type: Article

Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Phagocytosis / Lipopolysaccharides / Antimicrobial Cationic Peptides / Cathelicidins / Macrophages Limits: Animals Language: En Journal: Mol Immunol Year: 2024 Document type: Article