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Peptidomic analysis of skin secretions from Rana heckscheri and Rana okaloosae provides insight into phylogenetic relationships among frogs of the Aquarana species group
- Source :
- Regulatory Peptides, Regulatory Peptides, Elsevier, 2007, 138 (2-3), pp.87-93. ⟨10.1016/j.regpep.2006.08.007⟩
- Publication Year :
- 2007
- Publisher :
- HAL CCSD, 2007.
-
Abstract
- International audience; The members of the Aquarana (or Rana catesbeiana species group) form a monophyletic group comprising seven species: R. catesbeiana, Rana clamitans, Rana grylio, Rana virgatipes, Rana septentrionalis, Rana heckscheri and Rana okaloosae. Previous work has led to structural characterization of the antimicrobial peptides present in electrically-stimulated skin secretions from the first five species listed and this study presents the primary structures of orthologs from the river frog R. heckscheri and the Florida bog frog R. okaloosae. Peptidomic analysis of R. heckscheri and R. okaloosae skin secretions led to the identification of peptides with antimicrobial activity belonging to the ranalexin, ranatuerin-2, and temporin families. In addition, a peptide (GFLDIIKDTGKDFAVKILNNLKCKLAGGCPR) was isolated from R. okaloosae whose primary structure identified it as a member of the palustrin-2 family. Consistent with previous data based upon morphological analysis and comparisons of the nucleotide sequences of mitochondrial and ribosomal genes, cladistic analysis based upon a comparison of the amino acid sequences of antimicrobial peptides indicates a sister-group relationship between R. heckscheri and R. grylio and a close, but less well defined, phylogenetic relationship between R. okaloosae and R. clamitans.
- Subjects :
- Male
Ranidae
Physiology
MESH: Sequence Analysis, Protein
[SDV.NEU.NB]Life Sciences [q-bio]/Neurons and Cognition [q-bio.NC]/Neurobiology
Clinical Biochemistry
MESH: Amino Acid Sequence
[CHIM.THER]Chemical Sciences/Medicinal Chemistry
Biochemistry
Monophyly
0302 clinical medicine
Endocrinology
Sequence Analysis, Protein
MESH: Amphibian Proteins
[SDV.BC.IC]Life Sciences [q-bio]/Cellular Biology/Cell Behavior [q-bio.CB]
MESH: Proteins
MESH: Animals
Cloning, Molecular
MESH: Phylogeny
Chromatography, High Pressure Liquid
Phylogeny
Antibacterial agent
Skin
0303 health sciences
biology
integumentary system
MESH: Ranidae
Ecology
MESH: Peptides
MESH: Antimicrobial Cationic Peptides
Rana clamitans
Molecular Sequence Data
MESH: Sequence Alignment
Zoology
Peptides, Cyclic
Amphibian Proteins
Rana
03 medical and health sciences
Cellular and Molecular Neuroscience
Alkaloids
Species Specificity
MESH: Skin
Phylogenetics
MESH: Alkaloids
Animals
MESH: Species Specificity
MESH: Cloning, Molecular
Amino Acid Sequence
MESH: Chromatography, High Pressure Liquid
MESH: Peptides, Cyclic
030304 developmental biology
MESH: Molecular Sequence Data
Proteins
biology.organism_classification
Temporin
MESH: Male
MESH: Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
[SDV.SP.PHARMA]Life Sciences [q-bio]/Pharmaceutical sciences/Pharmacology
Rana grylio
Peptides
Frog Skin
Sequence Alignment
030217 neurology & neurosurgery
Antimicrobial Cationic Peptides
Subjects
Details
- Language :
- English
- ISSN :
- 01670115
- Database :
- OpenAIRE
- Journal :
- Regulatory Peptides, Regulatory Peptides, Elsevier, 2007, 138 (2-3), pp.87-93. ⟨10.1016/j.regpep.2006.08.007⟩
- Accession number :
- edsair.doi.dedup.....d119270057710b141696d2c83e085a93