1. Peptidomic analysis of skin secretions demonstrates that the allopatric populations of Xenopus muelleri (Pipidae) are not conspecific.
- Author
-
Mechkarska M, Ahmed E, Coquet L, Leprince J, Jouenne T, Vaudry H, King JD, and Conlon JM
- Subjects
- Africa, Eastern, Africa, Western, Amino Acid Sequence, Amphibian Proteins chemistry, Amphibian Proteins pharmacology, Animals, Antimicrobial Cationic Peptides chemistry, Antimicrobial Cationic Peptides pharmacology, Candida albicans drug effects, Candida albicans growth & development, Chromatography, High Pressure Liquid, Erythrocytes cytology, Erythrocytes metabolism, Escherichia coli drug effects, Escherichia coli growth & development, Female, Hemolysis drug effects, Humans, Male, Microbial Sensitivity Tests, Molecular Sequence Data, Phylogeny, Phylogeography, Skin chemistry, Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization, Staphylococcus aureus drug effects, Staphylococcus aureus growth & development, Xenopus genetics, Amphibian Proteins analysis, Antimicrobial Cationic Peptides analysis, Bodily Secretions chemistry, Genetic Speciation, Proteomics methods, Skin metabolism, Xenopus metabolism
- Abstract
Mueller's clawed frog Xenopus muelleri (Peters 1844) occupies two non-contiguous ranges in east and west Africa. The phylogenetic relationship between the two populations is unclear and it has been proposed that the western population represents a separate species. Peptidomic analysis of norepinephrine-stimulated skin secretions from X. muelleri from the eastern range resulted in the identification of five antimicrobial peptides structurally related to the magainins (magainin-M1 and -M2), xenopsin-precursor fragments (XPF-M1) and caerulein-precursor fragments (CPF-M1 and -M2) previously found in skin secretions of other Xenopus species. A cyclic peptide (WCPPMIPLCSRF.NH₂) containing the RFamide motif was also isolated that shows limited structural similarity to the tigerinins, previously identified only in frogs of the Dicroglossidae family. The components identified in skin secretions from X. muelleri from the western range comprised one magainin (magainin-MW1), one XPF peptide (XPF-MW1), two peptides glycine-leucine amide (PGLa-MW1 and -MW2), and three CPF peptides (CPF-MW1, -MW2 and -MW3). Comparison of the primary structures of these peptides suggest that western population of X. muelleri is more closely related to X. borealis than to X. muelleri consistent with its proposed designation as a separate species. The CPF peptides showed potent, broad-spectrum activity against reference strains of bacteria (MIC 3-25 μM), but were hemolytic against human erythrocytes., (Copyright © 2011 Elsevier Inc. All rights reserved.)
- Published
- 2011
- Full Text
- View/download PDF