Peptidomic analysis of the extensive array of host-defense peptides in skin secretions of the dodecaploid frog Xenopus ruwenzoriensis (Pipidae)

L Coqueta, J Kolodziejek, T Jouenne, N Nowotny, JD King, JM Conlon

Research output: Contribution to journalArticle

1 Citation (Scopus)

Abstract

The Uganda clawed frog Xenopus ruwenzoriensis with a karyotype of 2n = 108 is one of the very few vertebrates with dodecaploid status. Peptidomic analysis of norepinephrine-stimulated skin secretions from this species led to the isolation and structural characterization of 23 host-defense peptides belonging to the following families: magainin (3 peptides), peptide glycine-leucine-amide (PGLa; 6 peptides), xenopsin-precursor fragment (XPF; 3 peptides), caerulein precursor fragment (CPF; 8 peptides), and caerulein precursor fragment -related peptide (CPF-RP; 3 peptides). In addition, the secretions contained caerulein, identical to the peptide from Xenopus laevis, and two peptides that were identified as members of the trefoil factor family (TFF). The data indicate that silencing of the host-defense peptide genes following polyploidization has been appreciable and non-uniform. Consistent with data derived from comparison of nucleotide sequences of mitochrondrial and nuclear genes, cladistic analyses based upon the primary structures of the host-defense peptides provide support for an evolutionary scenario in which X. ruwenzoriensis arose from an allopolyploidization event involving an octoploid ancestor of the present-day frogs belonging to the Xenopus amieti species group and a tetraploid ancestor of Xenopus pygmaeus.
LanguageEnglish
Pages18-24
JournalComparative Biochemistry and Physiology - Part D: Genomics and Proteomics
Volume19C
DOIs
Publication statusPublished - 25 Aug 2016

Fingerprint

Pipidae
Xenopus
Anura
Skin
Peptides
Ceruletide
Magainins
Genes
Peptide Fragments
Uganda
Tetraploidy
Xenopus laevis

Keywords

  • antimicrobial peptide
  • frog skin
  • magainin
  • PGLa
  • procaerulein
  • proxenopsin
  • allopolyploidy
  • Xenopus

Cite this

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title = "Peptidomic analysis of the extensive array of host-defense peptides in skin secretions of the dodecaploid frog Xenopus ruwenzoriensis (Pipidae)",
abstract = "The Uganda clawed frog Xenopus ruwenzoriensis with a karyotype of 2n = 108 is one of the very few vertebrates with dodecaploid status. Peptidomic analysis of norepinephrine-stimulated skin secretions from this species led to the isolation and structural characterization of 23 host-defense peptides belonging to the following families: magainin (3 peptides), peptide glycine-leucine-amide (PGLa; 6 peptides), xenopsin-precursor fragment (XPF; 3 peptides), caerulein precursor fragment (CPF; 8 peptides), and caerulein precursor fragment -related peptide (CPF-RP; 3 peptides). In addition, the secretions contained caerulein, identical to the peptide from Xenopus laevis, and two peptides that were identified as members of the trefoil factor family (TFF). The data indicate that silencing of the host-defense peptide genes following polyploidization has been appreciable and non-uniform. Consistent with data derived from comparison of nucleotide sequences of mitochrondrial and nuclear genes, cladistic analyses based upon the primary structures of the host-defense peptides provide support for an evolutionary scenario in which X. ruwenzoriensis arose from an allopolyploidization event involving an octoploid ancestor of the present-day frogs belonging to the Xenopus amieti species group and a tetraploid ancestor of Xenopus pygmaeus.",
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language = "English",
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Peptidomic analysis of the extensive array of host-defense peptides in skin secretions of the dodecaploid frog Xenopus ruwenzoriensis (Pipidae). / Coqueta, L; Kolodziejek, J; Jouenne, T; Nowotny, N; King, JD; Conlon, JM.

In: Comparative Biochemistry and Physiology - Part D: Genomics and Proteomics, Vol. 19C, 25.08.2016, p. 18-24.

Research output: Contribution to journalArticle

TY - JOUR

T1 - Peptidomic analysis of the extensive array of host-defense peptides in skin secretions of the dodecaploid frog Xenopus ruwenzoriensis (Pipidae)

AU - Coqueta, L

AU - Kolodziejek, J

AU - Jouenne, T

AU - Nowotny, N

AU - King, JD

AU - Conlon, JM

PY - 2016/8/25

Y1 - 2016/8/25

N2 - The Uganda clawed frog Xenopus ruwenzoriensis with a karyotype of 2n = 108 is one of the very few vertebrates with dodecaploid status. Peptidomic analysis of norepinephrine-stimulated skin secretions from this species led to the isolation and structural characterization of 23 host-defense peptides belonging to the following families: magainin (3 peptides), peptide glycine-leucine-amide (PGLa; 6 peptides), xenopsin-precursor fragment (XPF; 3 peptides), caerulein precursor fragment (CPF; 8 peptides), and caerulein precursor fragment -related peptide (CPF-RP; 3 peptides). In addition, the secretions contained caerulein, identical to the peptide from Xenopus laevis, and two peptides that were identified as members of the trefoil factor family (TFF). The data indicate that silencing of the host-defense peptide genes following polyploidization has been appreciable and non-uniform. Consistent with data derived from comparison of nucleotide sequences of mitochrondrial and nuclear genes, cladistic analyses based upon the primary structures of the host-defense peptides provide support for an evolutionary scenario in which X. ruwenzoriensis arose from an allopolyploidization event involving an octoploid ancestor of the present-day frogs belonging to the Xenopus amieti species group and a tetraploid ancestor of Xenopus pygmaeus.

AB - The Uganda clawed frog Xenopus ruwenzoriensis with a karyotype of 2n = 108 is one of the very few vertebrates with dodecaploid status. Peptidomic analysis of norepinephrine-stimulated skin secretions from this species led to the isolation and structural characterization of 23 host-defense peptides belonging to the following families: magainin (3 peptides), peptide glycine-leucine-amide (PGLa; 6 peptides), xenopsin-precursor fragment (XPF; 3 peptides), caerulein precursor fragment (CPF; 8 peptides), and caerulein precursor fragment -related peptide (CPF-RP; 3 peptides). In addition, the secretions contained caerulein, identical to the peptide from Xenopus laevis, and two peptides that were identified as members of the trefoil factor family (TFF). The data indicate that silencing of the host-defense peptide genes following polyploidization has been appreciable and non-uniform. Consistent with data derived from comparison of nucleotide sequences of mitochrondrial and nuclear genes, cladistic analyses based upon the primary structures of the host-defense peptides provide support for an evolutionary scenario in which X. ruwenzoriensis arose from an allopolyploidization event involving an octoploid ancestor of the present-day frogs belonging to the Xenopus amieti species group and a tetraploid ancestor of Xenopus pygmaeus.

KW - antimicrobial peptide

KW - frog skin

KW - magainin

KW - PGLa

KW - procaerulein

KW - proxenopsin

KW - allopolyploidy

KW - Xenopus

U2 - 10.1016/j.cbd.2016.04.006

DO - 10.1016/j.cbd.2016.04.006

M3 - Article

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SP - 18

EP - 24

JO - Comparative Biochemistry and Physiology - Part D: Genomics and Proteomics

T2 - Comparative Biochemistry and Physiology - Part D: Genomics and Proteomics

JF - Comparative Biochemistry and Physiology - Part D: Genomics and Proteomics

SN - 1744-117X

ER -