TY - JOUR
T1 - Host-defense peptides from skin secretions of Fraser's clawed frog Xenopus fraseri (Pipidae)
T2 - Further insight into the evolutionary history of the Xenopodinae
AU - Conlon, J. Michael
AU - Mechkarska, Milena
AU - Kolodziejek, Jolanta
AU - Nowotny, Norbert
AU - Coquet, Laurent
AU - Leprince, Jérôme
AU - Jouenne, Thierry
AU - Vaudry, Hubert
N1 - Publisher Copyright:
© 2014 Elsevier Inc. All rights reserved.
PY - 2014/12
Y1 - 2014/12
N2 - Peptidomic analysis of norepinephrine-stimulated skin secretions of the tetraploid frog Xenopus fraseri Boulenger, 1905 (Pipidae) led to identification of 13 host-defense peptides. The primary structures of the peptides demonstrate that they belong to the magainin (3 peptides), peptide glycine-leucine-amide, PGLa (4 peptides), and xenopsin-precursor fragment, XPF (2 peptides) families, first identified in Xenopus laevis, together with caerulein precursor fragment-related peptides, CPF-RP (4 peptides), first identified in Silurana tropicalis. In addition, the secretions contain a molecular variant of xenopsin displaying the substitution Arg4 → Lys compared with X. laevis xenopsin and peptide glycine-tyrosine-amide (PGYa) (GRIIPIYPEFERVFA KKVYPLY.NH2) whose function is unknown. The most potent antimicrobial peptide identified is CPF-RP-F1 (GFGSVLGKALKFGANLL.NH2) with MIC = 12.5 μM against Staphylococcus aureus and 50 μM against Escherichia coli. On the basis of similarities in morphology and advertisement calls, X. fraseri has been placed in a species group that includes the octoploids Xenopus amieti and Xenopus andrei, and the tetraploid Xenopus pygmaeus. Cladistic analyses based upon the primary structures of magainin, PGLa, and CPF-RP peptides support a close evolutionary relationship between X. fraseri, X. amieti and X. andrei but suggest a more distant relationship with X. pygmaeus.
AB - Peptidomic analysis of norepinephrine-stimulated skin secretions of the tetraploid frog Xenopus fraseri Boulenger, 1905 (Pipidae) led to identification of 13 host-defense peptides. The primary structures of the peptides demonstrate that they belong to the magainin (3 peptides), peptide glycine-leucine-amide, PGLa (4 peptides), and xenopsin-precursor fragment, XPF (2 peptides) families, first identified in Xenopus laevis, together with caerulein precursor fragment-related peptides, CPF-RP (4 peptides), first identified in Silurana tropicalis. In addition, the secretions contain a molecular variant of xenopsin displaying the substitution Arg4 → Lys compared with X. laevis xenopsin and peptide glycine-tyrosine-amide (PGYa) (GRIIPIYPEFERVFA KKVYPLY.NH2) whose function is unknown. The most potent antimicrobial peptide identified is CPF-RP-F1 (GFGSVLGKALKFGANLL.NH2) with MIC = 12.5 μM against Staphylococcus aureus and 50 μM against Escherichia coli. On the basis of similarities in morphology and advertisement calls, X. fraseri has been placed in a species group that includes the octoploids Xenopus amieti and Xenopus andrei, and the tetraploid Xenopus pygmaeus. Cladistic analyses based upon the primary structures of magainin, PGLa, and CPF-RP peptides support a close evolutionary relationship between X. fraseri, X. amieti and X. andrei but suggest a more distant relationship with X. pygmaeus.
KW - Caerulein-precursor fragment
KW - Frog skin
KW - Host-defense peptide
KW - Magainin
KW - PGLa
UR - http://www.scopus.com/inward/record.url?scp=84908459860&partnerID=8YFLogxK
U2 - 10.1016/j.cbd.2014.10.001
DO - 10.1016/j.cbd.2014.10.001
M3 - Article
C2 - 25463057
AN - SCOPUS:84908459860
SN - 1744-117X
VL - 12
SP - 45
EP - 52
JO - Comparative Biochemistry and Physiology - Part D: Genomics and Proteomics
JF - Comparative Biochemistry and Physiology - Part D: Genomics and Proteomics
ER -