However, the numbers of paralogs from the octoploid frogs were not significantly greater than the corresponding numbers from the tetraploid frogs. The data indicate, therefore, that nonfunctionalization (gene deletion) has been the most common fate of duplicated antimicrobial peptide genes following polyploidization events in the Silurana and Xenopus lineages. All Xenopus antimicrobial peptides may be classified in the magainin, peptide glycine-leucine-amide (PGLa), caerulein-precursor fragment (CPF), and xenopsin-precursor fragment (XPF) families. borealis, and five from the tetraploid frog X. Caerulein is a decapeptide that contains the C-terminal four amino-acid sequence (Trp-Met-Asp-Phe-NH 2) that is conserved in vertebrate gastrin and CCK. tropicalis, nine from the tetraploid frog X. Abstract Caerulein was first purified and identified in the Australian frog Hyla caerulea in 1967 and has been detected in several frog species. glutamine (PGQ) 3) four caerulein precursor fragments (CPF 14) and 4) three. Under the same experimental conditions, seven orthologous antimicrobial peptides were previously isolated from the diploid frog S. of three semi-aquatic Litoria frog species L. In experiment 3, frogs were either injected with 80 nmol of. andrei components comprised two peptides from the magainin family, (magainin-AN1 and -AN2), two from the XPF family (XPF-AN1 and -AN2), two from the PGLa family(PGLa-AN1 and -AN2), and one caerulein-precursor fragment (CPF-AN1).The primary structures of these peptides indicate a close phylogenetic relationship between X. Caerulein precursor fragment (CPF) and PGLa (for peptide with amino-terminal glycine and. The CPF peptides showed potent, broad-spectrum antimicrobial activity. paratropicalis components comprised three peptides belonging to the caerulein-precursor fragment family (CPF-SP1, -SP2 and -SP3), two peptides from the xenopsin-precursor fragment family (XPF-SP1 and -SP2), and one peptide orthologous to peptide glycine-leucine-amide (PGLa-SP1). paratropicalis components comprised three peptides belonging to the caerulein-precursor fragment family (CPF-SP1, -SP2 and -SP3), two peptides from the xenopsin. Structural characterization demonstrated that the S. The sequence was composed of 705 bp of coding region, accounting for 234 amino. In addition, CPF-SE1 (GFLGPLLKLGLKGVAKVIPHLIPSRQQ), previously isolated from skin secretions of the tetraploid frog Silurana epitropicalis, produced a significant (P <0. andrei led to identification of multiple peptides with growth-inhibitory activity against Escherichia coli and Staphylococcus aureus. The complete nucleotide sequence of mRNA for caerulein precursor in the skin of Xenopus laevis was determined. Peptidomic analysis of norepinephrine-stimulated skin secretions of S. paratropicalis and a second polyploidization within the Xenopus lineage has produced the octoploid frog X. However, the very low antimicrobial activity of the magainin-AM1 and PGLa-AM2 paralogs suggests the possibility that certain peptides may have evolved toward a new, as yet undetermined, function (neofunctionalization).A putative genome duplication event within the Silurana lineage has given rise to the tetraploid frog S. The data indicate that nonfunctionalization has been the most common fate of duplicated antimicrobial peptide genes following the polyploidization events in the X. 29C.2).3 The precursor contains a signal peptide, an antimicrobial peptide called a caerulein precursor fragment (CPF), and mature caerulein (Fig. CFP-AM1 (GLGSVLGKALKIGANLL.NH2) was the most potent peptide present in the secretions and magainin-AM2 (GVSKILHSAGKFGKAFLGEIMKS) was the most abundant. Two peptides (magainin-AM1 and -AM2) are othologous to the magainins, two peptides (PGLa-AM1 and -AM2) orthologous to peptide glycine–leucine-amide, four peptides (CPF-AM1, -AM2, -AM3, -AM4) orthologous to caerulein-precursor fragments, and one peptide (XPF-AM1) structurally similar to xenopsin-precursor fragments were characterized. laevis (2n = 36) and the diploid frog Silurana (formerly Xenopus) tropicalis (2n = 20). amieti that showed structural similarity to peptides previously isolated from the tetraploid frog X. Nine peptides with differential antimicrobial activity against Escherichia coli and Staphylococcus aureus were isolated from norepinephrine-stimulated skin secretions of X. The Volcano clawed frog Xenopus amieti Kobel, du Pasquier, Fischberg, and Gloor, 1980, with a chromosome number of 2n = 72, is believed to have undergone two rounds of genome duplication since evolving from a diploid ancestor.
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