Affordable Access

Publisher Website

Characterization of the host-defense peptides from skin secretions of Merlin's clawed frogPseudhymenochirus merlini: Insights into phylogenetic relationships among the Pipidae

Authors
Journal
Comparative Biochemistry and Physiology Part D Genomics and Proteomics
1744-117X
Publisher
Elsevier
Volume
8
Issue
4
Identifiers
DOI: 10.1016/j.cbd.2013.10.002
Keywords
  • Antimicrobial Peptide
  • Frog Skin
  • Pipidae
  • Pseudhymenochirus
  • Hymenochirus

Abstract

Abstract 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=2.5μM) and Escherichia coli (MIC=10μM). 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.

There are no comments yet on this publication. Be the first to share your thoughts.