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Antimicrobial peptides with therapeutic potential from skin secretions of the Marsabit clawed frog Xenopus borealis (Pipidae)
- Source :
- Comparative Biochemistry and Physiology-Part C: Toxicology and Pharmacology, Comparative Biochemistry and Physiology-Part C: Toxicology and Pharmacology, Elsevier, 2010, 152 (4), pp.467-472. ⟨10.1016/j.cbpc.2010.07.007⟩
- Publication Year :
- 2010
- Publisher :
- HAL CCSD, 2010.
-
Abstract
- International audience; Nine peptides with differential growth inhibitory activity against Escherichia coli and Staphylococcus aureus were isolated from norepinephrine-stimulated skin secretions of the tetraploid frog Xenopus borealis Parker, 1936 (Pipidae). Structural characterization of the peptides demonstrated that they were orthologous to magainin-2 (1 peptide), peptide glycine-leucine-amide, PGLa (2 peptides), caerulein-precursor fragments, CPF (4 peptides), and xenopsin-precursor fragments, XPF (2 peptides), previously isolated from Xenopus laevis and X. amieti. In addition, a second magainin-related peptide (G**KFLHSAGKFGKAFLGEVMIG) containing a two amino acid residue deletion compared with magainin-2 was identified that had only weak antimicrobial activity. The peptide with the greatest potential for development into a therapeutically valuable anti-infective agent was CPF-B1 (GLGSLLGKAFKIGLKTVGKMMGGAPREQ) with MIC=5 microM against E. coli, MIC=5 microM against S. aureus, and MIC=25 microM against Candida albicans, and low hemolytic activity against human erythrocytes (LC(50)>200 microM). This peptide was also the most abundant antimicrobial peptide in the skin secretions. CPF-B1 was active against clinical isolates of the nosocomial pathogens, methicillin-resistant S. aureus (MRSA) and multidrug-resistant Acinetobacter baumannii (MDRAB) with MIC values in the range 4-8 microM.
- Subjects :
- Physiology
Health, Toxicology and Mutagenesis
Xenopus
[SDV.NEU.NB]Life Sciences [q-bio]/Neurons and Cognition [q-bio.NC]/Neurobiology
Antimicrobial peptides
Pipidae
MESH: Anti-Infective Agents
Peptide
[CHIM.THER]Chemical Sciences/Medicinal Chemistry
Xenopus Proteins
Toxicology
medicine.disease_cause
Biochemistry
Microbiology
03 medical and health sciences
Anti-Infective Agents
MESH: Skin
[SDV.BC.IC]Life Sciences [q-bio]/Cellular Biology/Cell Behavior [q-bio.CB]
medicine
Animals
MESH: Animals
MESH: Xenopus
Candida albicans
Escherichia coli
MESH: Xenopus Proteins
030304 developmental biology
Skin
chemistry.chemical_classification
0303 health sciences
biology
030306 microbiology
Xenopus borealis
MESH: Antimicrobial Cationic Peptides
Cell Biology
General Medicine
biology.organism_classification
Antimicrobial
3. Good health
chemistry
Staphylococcus aureus
[SDV.SP.PHARMA]Life Sciences [q-bio]/Pharmaceutical sciences/Pharmacology
Antimicrobial Cationic Peptides
Subjects
Details
- Language :
- English
- ISSN :
- 15320456
- Database :
- OpenAIRE
- Journal :
- Comparative Biochemistry and Physiology-Part C: Toxicology and Pharmacology, Comparative Biochemistry and Physiology-Part C: Toxicology and Pharmacology, Elsevier, 2010, 152 (4), pp.467-472. ⟨10.1016/j.cbpc.2010.07.007⟩
- Accession number :
- edsair.doi.dedup.....c889da5af0cd95d69381c7a61e115dda