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A novel endogenous antimicrobial peptide CAMP 211-225 derived from casein in human milk.
- Source :
-
Food & function [Food Funct] 2020 Mar 26; Vol. 11 (3), pp. 2291-2298. - Publication Year :
- 2020
-
Abstract
- A large number of bioactive peptides derived from breast milk have been identified to be multifunctional having anti-inflammatory, immunoregulatory and antimicrobial activities. Here, we report that an endogenous peptide located at β-casein 211-225 amino acid from human breast milk (hereafter called CAMP211-225) presents specific antimicrobial activity against pathogenic E. coli and Y. enterocolitica. CAMP211-225 is a novel peptide that occurs at higher levels in preterm milk than in term milk. The minimal inhibitory concentrations (MIC) of CAMP211-225 against E. coli and Y. enterocolitica are 3.125 μg ml-1 and 6.25 μg ml-1, respectively, and the antimicrobial activity of CAMP211-225 was also confirmed by a disk diffusion assay. Further studies using fluorescence staining, scanning electron microscopy and a DNA-binding assay revealed that CAMP211-225 kills bacteria through a membrane-disrupting mechanism, but not by binding to intracellular nucleic acids. Neonatal necrotizing enterocolitis (NEC) is a devastating gastrointestinal disease in neonatal intensive care units. In our study, CAMP211-225 administration effectively reduced ileal mucosa damage in an experimental NEC mice model. These results suggest that the antimicrobial peptide CAMP211-225 may have potential value in the prevention and treatment of neonatal infections.
- Subjects :
- Animals
Disease Models, Animal
Enterocolitis, Necrotizing microbiology
Escherichia coli drug effects
Humans
Ileum drug effects
Ileum microbiology
Mice
Yersinia enterocolitica drug effects
Anti-Bacterial Agents chemistry
Anti-Bacterial Agents isolation & purification
Anti-Bacterial Agents pharmacology
Caseins chemistry
Milk, Human chemistry
Pore Forming Cytotoxic Proteins chemistry
Pore Forming Cytotoxic Proteins isolation & purification
Pore Forming Cytotoxic Proteins pharmacology
Subjects
Details
- Language :
- English
- ISSN :
- 2042-650X
- Volume :
- 11
- Issue :
- 3
- Database :
- MEDLINE
- Journal :
- Food & function
- Publication Type :
- Academic Journal
- Accession number :
- 32104859
- Full Text :
- https://doi.org/10.1039/c9fo02813g