Peptidomic analysis of the extensive array of host-defense peptides in skin secretions of the dodecaploid frog Xenopus ruwenzoriensis (Pipidae).
The Uganda clawed frog Xenopus ruwenzoriensis with a karyotype of 2n=108 is one of the very few vertebrates with dodecaploid status. Peptidomic analysis of norepinephrine-stimulated skin secretions from this species led to the isolation and structural characterization of 23 host-defense peptides belonging to the following families: magainin (3 peptides), peptide glycine-leucine-amide (PGLa; 6 peptides), xenopsin precursor fragment (XPF; 3 peptides), caerulein precursor fragment (CPF; 8 peptides), and caerulein precursor fragment-related peptide (CPF-RP; 3 peptides). In addition, the secretions contained caerulein, identical to the peptide from Xenopus laevis, and two peptides that were identified as members of the trefoil factor family (TFF). The data indicate that silencing of the host-defense peptide genes following polyploidization has been appreciable and non-uniform. Consistent with data derived from comparison of nucleotide sequences of mitochrondrial and nuclear genes, cladistic analyses based upon the primary structures of the host-defense peptides provide support for an evolutionary scenario in which X. ruwenzoriensis arose from an allopolyploidization event involving an octoploid ancestor of the present-day frogs belonging to the Xenopus amieti species group and a tetraploid ancestor of Xenopus pygmaeus.
CNRS UMR 6270, University of Rouen, 76821 Mont-Saint-Aignan, France; PISSARO, Institute for Research and Innovation in Biomedicine (IRIB), University of Rouen, 76821 Mont-Saint-Aignan, France.
Laurent
L
Coquet
Viral Zoonoses, Emerging and Vector-Borne Infections Group, Institute of Virology, University of Veterinary Medicine, Veterinärplatz 1, A-1210 Vienna, Austria.
Jolanta
J
Kolodziejek
CNRS UMR 6270, University of Rouen, 76821 Mont-Saint-Aignan, France; PISSARO, Institute for Research and Innovation in Biomedicine (IRIB), University of Rouen, 76821 Mont-Saint-Aignan, France.
Thierry
T
Jouenne
Viral Zoonoses, Emerging and Vector-Borne Infections Group, Institute of Virology, University of Veterinary Medicine, Veterinärplatz 1, A-1210 Vienna, Austria.
Norbert
N
Nowotny
Rare Species Conservatory Foundation, St. Louis, MO 63110, USA.
Jay D
JD
King
SAAD Centre for Pharmacy and Diabetes, School of Biomedical Sciences, University of Ulster, Coleraine BT52 1SA, UK. Electronic address: m.conlon@ulster.ac.uk.
J Michael
JM
Conlon
D000818:Animals; D019143:Evolution, Molecular; D009638:Norepinephrine / Q000494:pharmacology*; D010446:Peptide Fragments / Q000032:analysis* / Q000302:isolation & purification; D010884:Pipidae / Q000378:metabolism*; D012867:Skin / Q000187:drug effects / Q000378:metabolism*; D014662:Vasoconstrictor Agents / Q000494:pharmacology; D029867:Xenopus Proteins / Q000378:metabolism*
D010446:Peptide Fragments; D014662:Vasoconstrictor Agents; D029867:Xenopus Proteins; D009638:Norepinephrine
Allopolyploidy; Antimicrobial peptide; Frog skin; Magainin; PGLa; Procaerulein; Proxenopsin; Xenopus