2010
DOI: 10.1016/j.peptides.2010.03.002
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Orthologs of magainin, PGLa, procaerulein-derived, and proxenopsin-derived peptides from skin secretions of the octoploid frog Xenopus amieti (Pipidae)

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Cited by 54 publications
(22 citation statements)
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“…A comparison of the amino acid sequences of procaerulein, promagainin, and proxenopsin, deduced from the nucleotide sequences of cDNAs, reveals significant structural similarity in the N-terminal regions of the precursors suggesting that the peptides may have evolved from a common ancestral gene by a series of duplication events [27]. Orthologs of magainin-1 and -2, PGLa, and CPF, and XPF have been identified in skin secretions of range of frog species belonging to the genus Xenopus ( X. amieti [28], X. andrei [29], X. borealis [30], X. clivii [31], X. lenduensis [32], X. muelleri and an incompletely characterized species from West Africa referred to as “ Xenopus new tetraploid 1” and provisionally designated X. muelleri West [33], X. petersii [32], X. pygmaeus [32], and X. victorianus [34]). Host-defense peptides have also been isolated from laboratory-generated F1 hybrids of X. laevis × X. muelleri [35] and X. laevis × X. borealis [36].…”
Section: Peptides With Antimicrobial Activitymentioning
confidence: 99%
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“…A comparison of the amino acid sequences of procaerulein, promagainin, and proxenopsin, deduced from the nucleotide sequences of cDNAs, reveals significant structural similarity in the N-terminal regions of the precursors suggesting that the peptides may have evolved from a common ancestral gene by a series of duplication events [27]. Orthologs of magainin-1 and -2, PGLa, and CPF, and XPF have been identified in skin secretions of range of frog species belonging to the genus Xenopus ( X. amieti [28], X. andrei [29], X. borealis [30], X. clivii [31], X. lenduensis [32], X. muelleri and an incompletely characterized species from West Africa referred to as “ Xenopus new tetraploid 1” and provisionally designated X. muelleri West [33], X. petersii [32], X. pygmaeus [32], and X. victorianus [34]). Host-defense peptides have also been isolated from laboratory-generated F1 hybrids of X. laevis × X. muelleri [35] and X. laevis × X. borealis [36].…”
Section: Peptides With Antimicrobial Activitymentioning
confidence: 99%
“…PGLa-AM1 from X. amieti shows broad spectrum bactericidal activity with MIC values ≤ 25 μM against reference strains of E. coli and S. aureus combined with very low toxicity to human red blood cells (LC 50 > 500 μM) [28]. PGLa-AM1 shows potent growth-inhibitory activity against clinical isolates of antibiotic-resistant A. baumannii , including strains that are resistant to colistin (MIC in the range 4–32 μM) [61].…”
Section: Peptides With Antimicrobial Activitymentioning
confidence: 99%
“…A comparison of the amino acid sequences of procaerulein, promagainin, and proxenopsin, deduced from the nucleotide sequences of cDNAs, reveals significant structural similarity in the N-terminal regions of the precursors suggesting that the peptides may have evolved from a common ancestral gene by a series of duplication events [43]. Orthologs of magainin-1 and -2, PGLa, caerulein-precursor fragment (CPF), and xenopsin-precursor fragment (XPF) have been identified in skin secretions of the tetraploid frog, X. borealis [44] and the octoploid frog, X. amieti [45]. A total of seven host-defense peptides were isolated from skin secretions of the diploid frog S. tropicalis [46].…”
Section: Pipidaementioning
confidence: 99%
“…5A, magainin-BM1 segregates in a clade containing magainin-AM1 and magainin-AN1 and magainin-BM2 is localized to a clade containing magainin-AM2 and magainin-AN2. Similarly, a close phylogenetic relationship between X. boumbaenis, X. amieti [5], and X. andrei [28] is suggested by similarities in the amino acid sequences of PGLa-BM1, PGLa-AM1 and PGLa-AN1; PGLa-BM2 and PGLa-AN2; and PGLa-BM3 and PGLa-AM2 (Fig. 5B).…”
Section: Discussionmentioning
confidence: 71%