Host-defense peptides from skin secretions of the tetraploid frogs Xenopus petersii and Xenopus pygmaeus, and the octoploid frog Xenopus lenduensis (Pipidae)
► Magainin, PGLa, and CPF peptides have been isolated from skin secretions of three Xenopus species. ► Xenopus petersii has a close but not conspecific phylogenetic relationships with Xenopus laevis. ► Xenopus pygmaeus does not belong in the laevis and muelleri species groups. ► Xenopus lenduensis e...
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| Published in: | Peptides (New York, N.Y. : 1980) Vol. 33; no. 1; pp. 35 - 43 |
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| Main Authors: | , , , , , , , |
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| Language: | English |
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| ISSN: | 0196-9781, 1873-5169, 1873-5169 |
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| Abstract | ► Magainin, PGLa, and CPF peptides have been isolated from skin secretions of three Xenopus species. ► Xenopus petersii has a close but not conspecific phylogenetic relationships with Xenopus laevis. ► Xenopus pygmaeus does not belong in the laevis and muelleri species groups. ► Xenopus lenduensis expresses the full complement of four PGLa genes. ► CPF peptides show the greatest antimicrobial activity.
Peptidomic analysis of norepinephrine-stimulated skin secretions led to the identification of host-defense peptides belonging to the magainin, peptide glycine-leucine-amide (PGLa), and caerulein precursor fragment (CPF) families from the tetraploid frogs, Xenopus petersii (Peters’ clawed frog) and Xenopus pygmaeus (Bouchia clawed frog), and the octoploid frog Xenopus lenduensis (Lendu Plateau clawed frog). Xenopsin-precursor fragment (XPF) peptides were not detected. The primary structures of the antimicrobial peptides from X. petersii demonstrate a close, but not conspecific relationship, with Xenopus laevis whereas the X. pygmaeus peptides show appreciable variation from previously characterized orthologs from other Xenopus species. Polyploidization events within the Xenopodinae (Silurana+Xenopus) are associated with extensive gene silencing (nonfunctionization) but unexpectedly the full complement of four PGLa paralogs were isolated from X. lenduendis secretions. Consistent with previous data, the CPF peptides showed the highest growth-inhibitory activity against bacteria with CPF-PG1 (GFGSLLGKALKIGTNLL.NH2) from X. pygmaeus combining high antimicrobial potency against Staphylococcus aureus (MIC=6μM) with relatively low hemolytic activity (LC50=145μM). |
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| AbstractList | Peptidomic analysis of norepinephrine-stimulated skin secretions led to the identification of host-defense peptides belonging to the magainin, peptide glycine-leucine-amide (PGLa), and caerulein precursor fragment (CPF) families from the tetraploid frogs, Xenopus petersii (Peters’ clawed frog) and Xenopus pygmaeus (Bouchia clawed frog), and the octoploid frog Xenopus lenduensis (Lendu Plateau clawed frog). Xenopsin-precursor fragment (XPF) peptides were not detected. The primary structures of the antimicrobial peptides from X. petersii demonstrate a close, but not conspecific relationship, with Xenopus laevis whereas the X. pygmaeus peptides show appreciable variation from previously characterized orthologs from other Xenopus species. Polyploidization events within the Xenopodinae (Silurana+Xenopus) are associated with extensive gene silencing (nonfunctionization) but unexpectedly the full complement of four PGLa paralogs were isolated from X. lenduendis secretions. Consistent with previous data, the CPF peptides showed the highest growth-inhibitory activity against bacteria with CPF-PG1 (GFGSLLGKALKIGTNLL.NH₂) from X. pygmaeus combining high antimicrobial potency against Staphylococcus aureus (MIC=6μM) with relatively low hemolytic activity (LC₅₀=145μM). Peptidomic analysis of norepinephrine-stimulated skin secretions led to the identification of host-defense peptides belonging to the magainin, peptide glycine-leucine-amide (PGLa), and caerulein precursor fragment (CPF) families from the tetraploid frogs, Xenopus petersii (Peters' clawed frog) and Xenopus pygmaeus (Bouchia clawed frog), and the octoploid frog Xenopus lenduensis (Lendu Plateau clawed frog). Xenopsin-precursor fragment (XPF) peptides were not detected. The primary structures of the antimicrobial peptides from X. petersii demonstrate a close, but not conspecific relationship, with Xenopus laevis whereas the X. pygmaeus peptides show appreciable variation from previously characterized orthologs from other Xenopus species. Polyploidization events within the Xenopodinae (Silurana + Xenopus) are associated with extensive gene silencing (nonfunctionization) but unexpectedly the full complement of four PGLa paralogs were isolated from X. lenduendis secretions. Consistent with previous data, the CPF peptides showed the highest growth-inhibitory activity against bacteria with CPF-PG1 (GFGSLLGKALKIGTNLL.NH2) from X. pygmaeus combining high antimicrobial potency against Staphylococcus aureus (MIC = 6 mu M) with relatively low hemolytic activity (LC50 = 145 mu M). Peptidomic analysis of norepinephrine-stimulated skin secretions led to the identification of host-defense peptides belonging to the magainin, peptide glycine-leucine-amide (PGLa), and caerulein precursor fragment (CPF) families from the tetraploid frogs, Xenopus petersii (Peters' clawed frog) and Xenopus pygmaeus (Bouchia clawed frog), and the octoploid frog Xenopus lenduensis (Lendu Plateau clawed frog). Xenopsin-precursor fragment (XPF) peptides were not detected. The primary structures of the antimicrobial peptides from X. petersii demonstrate a close, but not conspecific relationship, with Xenopus laevis whereas the X. pygmaeus peptides show appreciable variation from previously characterized orthologs from other Xenopus species. Polyploidization events within the Xenopodinae (Silurana+Xenopus) are associated with extensive gene silencing (nonfunctionization) but unexpectedly the full complement of four PGLa paralogs were isolated from X. lenduendis secretions. Consistent with previous data, the CPF peptides showed the highest growth-inhibitory activity against bacteria with CPF-PG1 (GFGSLLGKALKIGTNLL.NH(2)) from X. pygmaeus combining high antimicrobial potency against Staphylococcus aureus (MIC=6 μM) with relatively low hemolytic activity (LC(50)=145 μM). ► Magainin, PGLa, and CPF peptides have been isolated from skin secretions of three Xenopus species. ► Xenopus petersii has a close but not conspecific phylogenetic relationships with Xenopus laevis. ► Xenopus pygmaeus does not belong in the laevis and muelleri species groups. ► Xenopus lenduensis expresses the full complement of four PGLa genes. ► CPF peptides show the greatest antimicrobial activity. Peptidomic analysis of norepinephrine-stimulated skin secretions led to the identification of host-defense peptides belonging to the magainin, peptide glycine-leucine-amide (PGLa), and caerulein precursor fragment (CPF) families from the tetraploid frogs, Xenopus petersii (Peters’ clawed frog) and Xenopus pygmaeus (Bouchia clawed frog), and the octoploid frog Xenopus lenduensis (Lendu Plateau clawed frog). Xenopsin-precursor fragment (XPF) peptides were not detected. The primary structures of the antimicrobial peptides from X. petersii demonstrate a close, but not conspecific relationship, with Xenopus laevis whereas the X. pygmaeus peptides show appreciable variation from previously characterized orthologs from other Xenopus species. Polyploidization events within the Xenopodinae (Silurana+Xenopus) are associated with extensive gene silencing (nonfunctionization) but unexpectedly the full complement of four PGLa paralogs were isolated from X. lenduendis secretions. Consistent with previous data, the CPF peptides showed the highest growth-inhibitory activity against bacteria with CPF-PG1 (GFGSLLGKALKIGTNLL.NH2) from X. pygmaeus combining high antimicrobial potency against Staphylococcus aureus (MIC=6μM) with relatively low hemolytic activity (LC50=145μM). Peptidomic analysis of norepinephrine-stimulated skin secretions led to the identification of host-defense peptides belonging to the magainin, peptide glycine-leucine-amide (PGLa), and caerulein precursor fragment (CPF) families from the tetraploid frogs, Xenopus petersii (Peters' clawed frog) and Xenopus pygmaeus (Bouchia clawed frog), and the octoploid frog Xenopus lenduensis (Lendu Plateau clawed frog). Xenopsin-precursor fragment (XPF) peptides were not detected. The primary structures of the antimicrobial peptides from X. petersii demonstrate a close, but not conspecific relationship, with Xenopus laevis whereas the X. pygmaeus peptides show appreciable variation from previously characterized orthologs from other Xenopus species. Polyploidization events within the Xenopodinae (Silurana+Xenopus) are associated with extensive gene silencing (nonfunctionization) but unexpectedly the full complement of four PGLa paralogs were isolated from X. lenduendis secretions. Consistent with previous data, the CPF peptides showed the highest growth-inhibitory activity against bacteria with CPF-PG1 (GFGSLLGKALKIGTNLL.NH(2)) from X. pygmaeus combining high antimicrobial potency against Staphylococcus aureus (MIC=6 μM) with relatively low hemolytic activity (LC(50)=145 μM).Peptidomic analysis of norepinephrine-stimulated skin secretions led to the identification of host-defense peptides belonging to the magainin, peptide glycine-leucine-amide (PGLa), and caerulein precursor fragment (CPF) families from the tetraploid frogs, Xenopus petersii (Peters' clawed frog) and Xenopus pygmaeus (Bouchia clawed frog), and the octoploid frog Xenopus lenduensis (Lendu Plateau clawed frog). Xenopsin-precursor fragment (XPF) peptides were not detected. The primary structures of the antimicrobial peptides from X. petersii demonstrate a close, but not conspecific relationship, with Xenopus laevis whereas the X. pygmaeus peptides show appreciable variation from previously characterized orthologs from other Xenopus species. Polyploidization events within the Xenopodinae (Silurana+Xenopus) are associated with extensive gene silencing (nonfunctionization) but unexpectedly the full complement of four PGLa paralogs were isolated from X. lenduendis secretions. Consistent with previous data, the CPF peptides showed the highest growth-inhibitory activity against bacteria with CPF-PG1 (GFGSLLGKALKIGTNLL.NH(2)) from X. pygmaeus combining high antimicrobial potency against Staphylococcus aureus (MIC=6 μM) with relatively low hemolytic activity (LC(50)=145 μM). |
| Author | King, Jay D. Vaudry, Hubert Jouenne, Thierry Takada, Koji Mechkarska, Milena Coquet, Laurent Leprince, Jérôme Conlon, J. Michael |
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| Cites_doi | 10.2741/3033 10.1016/j.tig.2004.09.001 10.1016/S0014-5793(97)01266-0 10.1534/genetics.106.069690 10.1016/S0014-5793(97)00055-0 10.1016/j.peptides.2003.08.023 10.1073/pnas.84.15.5449 10.1016/j.ygcen.2011.03.022 10.1016/j.peptides.2011.05.025 10.1016/j.ympev.2004.04.018 10.1007/s00441-010-1014-4 10.1016/S0021-9258(19)57220-9 10.1080/00222933608655232 10.1016/j.ymeth.2007.01.004 10.1016/j.peptides.2010.03.002 10.1016/0022-2836(82)90515-0 10.5962/bhl.part.79511 10.1007/978-1-60761-594-1_19 10.1093/molbev/msi104 10.1111/j.1469-7998.2010.00769.x 10.1038/nsb0694-399 |
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| Keywords | Allopolyploidy Xenopus Frog skin Procaerulein PGLa Magainin Antimicrobial peptide |
| Language | English |
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| Snippet | ► Magainin, PGLa, and CPF peptides have been isolated from skin secretions of three Xenopus species. ► Xenopus petersii has a close but not conspecific... Peptidomic analysis of norepinephrine-stimulated skin secretions led to the identification of host-defense peptides belonging to the magainin, peptide... |
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| SubjectTerms | Allopolyploidy Amino Acid Sequence Animals Antimicrobial Cationic Peptides Antimicrobial Cationic Peptides - chemistry Antimicrobial Cationic Peptides - isolation & purification Antimicrobial Cationic Peptides - pharmacology Antimicrobial peptide antimicrobial peptides Anura Bacteria Cell Behavior Cellular Biology Ceruletide Ceruletide - chemistry Chemical Sciences Complement CPF Erythrocytes Erythrocytes - drug effects Fragmentation Frog skin Frogs gene silencing Genes hemolysis Hemolytic Agents Hemolytic Agents - pharmacology Humans Life Sciences Magainin Magainins Magainins - chemistry Medicinal Chemistry Microbial Sensitivity Tests Molecular Sequence Data Neurobiology Neurons and Cognition Peptides Peptides - chemistry PGLa Pharmaceutical sciences Pharmacology Pipidae plateaus Polyploidy Procaerulein Protein Precursors Protein Precursors - chemistry Secretions Skin Skin - secretion Staphylococcus aureus Staphylococcus aureus - drug effects Structural Homology, Protein Tetraploidy Xenopus Xenopus - genetics Xenopus laevis Xenopus Proteins Xenopus Proteins - chemistry Xenopus Proteins - isolation & purification |
| Title | Host-defense peptides from skin secretions of the tetraploid frogs Xenopus petersii and Xenopus pygmaeus, and the octoploid frog Xenopus lenduensis (Pipidae) |
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