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<lom:catalog>phaidra.vetmeduni.ac.at</lom:catalog>

  
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<lom:identifier>
  
<lom:catalog>DOI</lom:catalog>

  
<lom:entry>
  
<lom:langstring xml:lang="x-none">10.1016/j.cbd.2023.101069</lom:langstring>

  
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</lom:identifier>

  
<lom:title>
  
<lom:langstring xml:lang="en">Peptidomic analysis of the host-defense peptides in skin secretions of the Amazon River frog Lithobates palmipes (Ranidae)</lom:langstring>

  
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<lom:description>
  
<lom:langstring xml:lang="en">Skin secretions of certain frog species represent a source of host-defense peptides (HDPs) with therapeutic potential and their primary structures provide insight into taxonomic and phylogenetic relationships. Peptidomic analysis was used to characterize the HDPs in norepinephrine-stimulated skin secretions from the Amazon River frog Lithobates palmipes (Ranidae) collected in Trinidad. A total of ten peptides were purified and identified on the basis of amino acid similarity as belonging to the ranatuerin-2 family (ranatuerin-2PMa, -2PMb, -2PMc, and-2PMd), the brevinin-1 family (brevinin-1PMa, -1PMb, -1PMc and des(8-14)brevinin-1PMa) and the temporin family (temporin-PMa in C-terminally amidated and non-amidated forms). Deletion of the sequence VAAKVLP from brevinin-1PMa (FLPLIAGVAAKVLPKIFCAISKKC) in des[(8-14)brevinin-1PMa resulted in a 10-fold decrease in potency against Staphylococcus aureus (MIC = 31 μM compared with 3 μM) and a &gt; 50-fold decrease in hemolytic activity but potency against Echerichia coli was maintained (MIC = 62.5 μM compared with 50 μM). Temporin-PMa (FLPFLGKLLSGIF.NH2) inhibited growth of S. aureus (MIC = 16 μM) but the non-amidated form of the peptide lacked antimicrobial activity. Cladistic analysis based upon the primary structures of ranaturerin-2 peptides supports the division of New World frogs of the family Ranidae into the genera Lithobates and Rana. A sister-group relationship between L. palmipes and Warszewitsch&#39;s frog Lithobates warszewitschii is indicated within a clade that includes the Tarahumara frog Lithobates tarahumarae. The study has provided further evidence that peptidomic analysis of HDPs in frog skin secretions is a valuable approach to elucidation of the evolutionary history of species within a particular genus.</lom:langstring>

  
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<lom:language>eng</lom:language>

  
<lom:keyword>
  
<lom:langstring xml:lang="en">Antimicrobial Peptides; Phylogeny; Amphibia; Proline; Tree</lom:langstring>

  
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<lom:datetime>2024-08-12T10:08:50.358Z</lom:datetime>

  
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<lom:vcard>BEGIN:VCARD
VERSION:3.0
N:Mechkarska;Milena;
FN:Milena Mechkarska
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<lom:vcard>BEGIN:VCARD
VERSION:3.0
N:Conlon;J. Michael;
FN:J. Michael Conlon
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<lom:vcard>BEGIN:VCARD
VERSION:3.0
N:Nowotny;Norbert;
FN:Norbert Nowotny
X-ORCID:https://orcid.org/0000-0002-3548-571X
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<lom:vcard>BEGIN:VCARD
VERSION:3.0
N:Jouenne;Thierry;
FN:Thierry Jouenne
END:VCARD</lom:vcard>

  
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<lom:vcard>BEGIN:VCARD
VERSION:3.0
N:Leprince;Jérôme;
FN:Jérôme Leprince
END:VCARD</lom:vcard>

  
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<lom:vcard>BEGIN:VCARD
VERSION:3.0
N:Coquet;Laurent;
FN:Laurent Coquet
END:VCARD</lom:vcard>

  
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<lom:vcard>BEGIN:VCARD
VERSION:3.0
N:Barran;Gervonne;
FN:Gervonne Barran
END:VCARD</lom:vcard>

  
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<lom:vcard>BEGIN:VCARD
VERSION:3.0
N:Kolodziejek;Jolanta;
FN:Jolanta Kolodziejek
X-ORCID:https://orcid.org/0000-0001-5736-3644
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