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...

Full description

Saved in:
Bibliographic Details
Published in:Peptides (New York, N.Y. : 1980) Vol. 33; no. 1; pp. 35 - 43
Main Authors: King, Jay D., Mechkarska, Milena, Coquet, Laurent, Leprince, Jérôme, Jouenne, Thierry, Vaudry, Hubert, Takada, Koji, Conlon, J. Michael
Format: Journal Article
Language:English
Published: United States Elsevier Inc 01.01.2012
Elsevier
Subjects:
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
Allopolyploidy
Xenopus
Frog skin
Procaerulein
PGLa
Magainin
Antimicrobial peptide
ISSN:0196-9781, 1873-5169, 1873-5169
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:► 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).
Bibliography:http://dx.doi.org/10.1016/j.peptides.2011.11.015
ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
content type line 23
ISSN:0196-9781
1873-5169
1873-5169
DOI:10.1016/j.peptides.2011.11.015