TY - JOUR
T1 - Host defense peptides from Lithobates forreri, Hylarana luctuosa, and Hylarana signata (Ranidae)
T2 - Phylogenetic relationships inferred from primary structures of ranatuerin-2 and brevinin-2 peptides
AU - Conlon, J. Michael
AU - Kolodziejek, Jolanta
AU - Mechkarska, Milena
AU - Coquet, Laurent
AU - Leprince, Jérôme
AU - Jouenne, Thierry
AU - Vaudry, Hubert
AU - Nielsen, Per F.
AU - Nowotny, Norbert
AU - King, Jay D.
N1 - Funding Information:
This work was supported by a Faculty Support Grant and a NRF/University grant from U.A.E. University and by the Terry Fox Fund for Cancer Research . The authors thank Teya King for help in collecting the frog species and Laurey Steinke and Michele Fontaine (University of Nebraska Medical Center, Omaha, NE) for amino acid composition analysis.
PY - 2014/3
Y1 - 2014/3
N2 - 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.
AB - 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.
KW - Antimicrobial peptide Lithobates
KW - Brevinin-2
KW - Hylarana
KW - Phylogeny
KW - Ranatuerin-2
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UR - http://www.scopus.com/inward/citedby.url?scp=84893137205&partnerID=8YFLogxK
U2 - 10.1016/j.cbd.2014.01.002
DO - 10.1016/j.cbd.2014.01.002
M3 - Article
C2 - 24463457
AN - SCOPUS:84893137205
SN - 1744-117X
VL - 9
SP - 49
EP - 57
JO - Comparative Biochemistry and Physiology - Part D: Genomics and Proteomics
JF - Comparative Biochemistry and Physiology - Part D: Genomics and Proteomics
IS - 1
ER -