Host defense peptides from Lithobates forreri, Hylarana luctuosa, and Hylarana signata (Ranidae): phylogenetic relationships inferred from primary structures of ranatuerin-2 and brevinin-2 peptides.
The primary structures of host-defense peptides present in frog skin secretions constitute useful molecular markers for establishing taxonomic classifications and investigating phylogenetic relationships between species within a particular genus. Peptidomic analysis has led to the characterization of multiple host-defense peptides in norepinephrine-stimulated skin secretions of three species of frogs from the family Ranidae: Lithobates forreri (Boulenger, 1883), Hylarana luctuosa (Peters, 1871), and Hylarana signata (Günther, 1872). The L. forreri secretions contain ranatuerin-2 (2 peptides), brevinin-1 (4 peptides), and temporin (1 peptide). The H. luctuosa secretions contain brevinin-2 (4 peptides), esculentin-1 (1 peptide), esculentin-2 (1 peptide), palustrin-2 (2 peptides), and temporin (2 peptides). The H. signata secretions contain brevinin-2 (4 peptides), brevinin-1 (5 peptides), palustrin-2 (1 peptide), and temporin (2 peptides). Cladistic analysis based upon the primary structures of 44 ranatuerin-2 peptides from 20 Lithobates species indicates a close phylogenetic relationship between L. forreri, Lithobates onca, and Lithobates yavapaiensis. A similar cladistic analysis based upon the primary structures of 27 brevinin-2 peptides from 8 Hylarana species provides support for a close phylogenetic relationship between H. signata and Hylarana picturata, while showing that the species are not conspecific, with H. luctuosa more distantly related.
Department of Biochemistry, College of Medicine and Health Sciences, United Arab Emirates University, 17666 Al-Ain, United Arab Emirates. Electronic address: jmconlon@uaeu.ac.ae.
J Michael
JM
Conlon
Viral Zoonoses, Emerging and Vector-Borne Infections Group, Institute of Virology, Department of Pathobiology, University of Veterinary Medicine, Veterinärplatz 1, A-1210 Vienna, Austria.
Jolanta
J
Kolodziejek
Department of Biochemistry, College of Medicine and Health Sciences, United Arab Emirates University, 17666 Al-Ain, United Arab Emirates.
Milena
M
Mechkarska
PISSARO, Institute for Research and Innovation in Biomedicine (IRIB), University of Rouen, 76821 Mont-Saint-Aignan, France; CNRS UMR 6270, University of Rouen, 76821 Mont-Saint-Aignan, France.
Laurent
L
Coquet
PISSARO, Institute for Research and Innovation in Biomedicine (IRIB), University of Rouen, 76821 Mont-Saint-Aignan, France; INSERM U-982, PRIMACEN, University of Rouen, 76821 Mont-Saint-Aignan, France.
Jérôme
J
Leprince
PISSARO, Institute for Research and Innovation in Biomedicine (IRIB), University of Rouen, 76821 Mont-Saint-Aignan, France; CNRS UMR 6270, University of Rouen, 76821 Mont-Saint-Aignan, France.
Thierry
T
Jouenne
PISSARO, Institute for Research and Innovation in Biomedicine (IRIB), University of Rouen, 76821 Mont-Saint-Aignan, France; INSERM U-982, PRIMACEN, University of Rouen, 76821 Mont-Saint-Aignan, France.
Hubert
H
Vaudry
Protein Science, Novo Nordisk A/S, 2760 Maalöv, Denmark.
Per F
PF
Nielsen
Viral Zoonoses, Emerging and Vector-Borne Infections Group, Institute of Virology, Department of Pathobiology, 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
D000595:Amino Acid Sequence; D029845:Amphibian Proteins / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification / Q000494:pharmacology; D000818:Animals; D000900:Anti-Bacterial Agents / Q000737:chemistry* / Q000302:isolation & purification / Q000378:metabolism / Q000494:pharmacology; D023181:Antimicrobial Cationic Peptides / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification / Q000494:pharmacology; D001419:Bacteria / Q000187:drug effects; D001424:Bacterial Infections / Q000188:drug therapy; D008297:Male; D008826:Microbial Sensitivity Tests; D008969:Molecular Sequence Data; D010802:Phylogeny; D011506:Proteins / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification / Q000494:pharmacology; D011898:Ranidae / Q000235:genetics*; D012867:Skin / Q000737:chemistry
D029845:Amphibian Proteins; D000900:Anti-Bacterial Agents; D023181:Antimicrobial Cationic Peptides; D011506:Proteins; C121230:ranatuerin; C104501:temporin
Antimicrobial peptide Lithobates; Brevinin-2; Hylarana; Phylogeny; Ranatuerin-2