TY - JOUR
T1 - Characterization of the host-defense peptides from skin secretions of Merlin's clawed frog Pseudhymenochirus merlini
T2 - Insights into phylogenetic relationships among the Pipidae
AU - Conlon, J. Michael
AU - Prajeep, Manju
AU - Mechkarska, Milena
AU - Coquet, Laurent
AU - Leprince, Jérôme
AU - Jouenne, Thierry
AU - Vaudry, Hubert
AU - King, Jay D.
N1 - Funding Information:
This work was supported by the Terry Fox Fund for Cancer Research , a Faculty Support Grant and a University Research Grant from U.A.E. University . The authors thank Noémio Sousa for supplying the captive-bred frogs.
PY - 2013
Y1 - 2013
N2 - The family Pipidae comprises the genera Hymenochirus, Pipa, Pseudhymenochirus, Silurana, and Xenopus but phylogenetic relationships within the family are unclear. Peptidomic analysis of norepinephrine-stimulated skin secretions from Pseudhymenochirus merlini Chabanaud, 1920, the single species within the genus Pseudhymenochirus, led to identification of 13 host-defense peptides with antimicrobial activity. Two peptides (hymenochirin-1Pa and -1Pb) show structural similarity to hymenochirin-1B from Hymenochirus boettgeri and eight peptides (hymenochirin-5Pa, -5Pb, -5Pc, -5Pd, -5Pe, -5Pf, 5Pg and -5Ph) are structurally similar to each other and to hymenochirin-5B from H. boettgeri. Two peptides differing by a single amino acid (IKIPSFFRNILKKVGKEAVSLM/I AGALKQS), termed pseudhymenochirin-1Pa and -1Pb, and pseudhymenochirin-2Pa (GIFPIFAKLLGKVIKVASSLISKGRTE) do not resemble host-defense peptides previously isolated from pipid frogs. Hymenochirin-5Pe was the most abundant peptide in the secretions and hymenochirin-1Pa the most potent against Staphylococcus aureus (MIC = 2.5 μM) and Escherichia coli (MIC = 10 μM). The data support a close phylogenetic relationship between Hymenochirus and Pseudhymenochirus that is distinct from the Xenopodinae (Xenopus + Silurana) clade with Pipa sister-group to all other extant pipids.
AB - The family Pipidae comprises the genera Hymenochirus, Pipa, Pseudhymenochirus, Silurana, and Xenopus but phylogenetic relationships within the family are unclear. Peptidomic analysis of norepinephrine-stimulated skin secretions from Pseudhymenochirus merlini Chabanaud, 1920, the single species within the genus Pseudhymenochirus, led to identification of 13 host-defense peptides with antimicrobial activity. Two peptides (hymenochirin-1Pa and -1Pb) show structural similarity to hymenochirin-1B from Hymenochirus boettgeri and eight peptides (hymenochirin-5Pa, -5Pb, -5Pc, -5Pd, -5Pe, -5Pf, 5Pg and -5Ph) are structurally similar to each other and to hymenochirin-5B from H. boettgeri. Two peptides differing by a single amino acid (IKIPSFFRNILKKVGKEAVSLM/I AGALKQS), termed pseudhymenochirin-1Pa and -1Pb, and pseudhymenochirin-2Pa (GIFPIFAKLLGKVIKVASSLISKGRTE) do not resemble host-defense peptides previously isolated from pipid frogs. Hymenochirin-5Pe was the most abundant peptide in the secretions and hymenochirin-1Pa the most potent against Staphylococcus aureus (MIC = 2.5 μM) and Escherichia coli (MIC = 10 μM). The data support a close phylogenetic relationship between Hymenochirus and Pseudhymenochirus that is distinct from the Xenopodinae (Xenopus + Silurana) clade with Pipa sister-group to all other extant pipids.
KW - Antimicrobial peptide
KW - Frog skin
KW - Hymenochirus
KW - Pipidae
KW - Pseudhymenochirus
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U2 - 10.1016/j.cbd.2013.10.002
DO - 10.1016/j.cbd.2013.10.002
M3 - Article
C2 - 24212286
AN - SCOPUS:84887050690
SN - 1744-117X
VL - 8
SP - 352
EP - 357
JO - Comparative Biochemistry and Physiology - Part D: Genomics and Proteomics
JF - Comparative Biochemistry and Physiology - Part D: Genomics and Proteomics
IS - 4
ER -