Antimicrobial peptides from the skin of the Tsushima brown frog Rana tsushimensis

Conlon, J. Michael; Al-Ghaferi, Nadia; Abraham, Bency; Sonnevend, Ágnes; Coquet, Laurent; Leprince, Jérôme; Jouenne, Thierry; Vaudry, Hubert; Iwamuro, Shawichi

doi:10.1016/j.cbpc.2005.11.022

Cited by 27 publications

(10 citation statements)

References 30 publications

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“…Seq 21 comprised 63% hydrophobic residues and showed a tendency to form α-helices. The sequence presented similarity with the temporins 1TSa (46%), PRa (43%), 1M (43%), 1Ec (43%), and 1AUa (43%). ,− …”

Section: Resultsmentioning

confidence: 99%

Antimicrobial Peptides from Skin Secretions of Hypsiboas pulchellus (Anura: Hylidae)

Siano

Húmpola

Oliveira³

et al. 2014

J. Nat. Prod.

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The skin of many amphibians produces a large repertoire of antimicrobial peptides that are crucial in the first line of defense against microbial invasion. Despite the immense richness of wild amphibians in Argentina, knowledge about peptides with antimicrobial properties is limited to a few species. Here we used LC-MS-MS to analyze samples of Hypsiboas pulchellus skin with the aim to identify antimicrobial peptides in the mass range of 1000 to 2000 Da. Twenty-three novel sequences were identified by MS, three of which were selected for chemical synthesis and further studies. The three synthetic peptides, named P1-Hp-1971, P2-Hp-1935, and P3-Hp-1891, inhibited the growth of two ATCC strains: Escherichia coli (MIC: 16, 33, and 17 μM, respectively) and Staphylococcus aureus (MIC: 8, 66, and 17 μM, respectively). P1-Hp-1971 and P3-Hp-1891 were the most active peptides. P1-Hp-1971, which showed the highest therapeutic indices (40 for E. coli and 80 for S. aureus), is a proline-glycine-rich peptide with a highly unordered structure, while P3-Hp-1891 adopts an amphipathic α-helical structure in the presence of 2,2,2-trifluoroethanol and anionic liposomes. This is the first peptidomic study of Hypsiboas pulchellus skin secretions to allow the identification of antimicrobial peptides.

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Section: Resultsmentioning

confidence: 99%

Antimicrobial Peptides from Skin Secretions of Hypsiboas pulchellus (Anura: Hylidae)

Siano

Húmpola

Oliveira³

et al. 2014

J. Nat. Prod.

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“…HDPs have been isolated from 16 different species ( Table 1 and Table 2 ). Common antimicrobial peptide families that were identified from this genus include Brevinin 1 and 2, Ranateurin, and Temporin 1 [ 61 , 62 , 63 , 64 , 65 , 66 , 67 , 68 , 69 , 70 , 71 , 72 , 73 , 74 , 75 ]. Temporin 1 from R. chensinensis exhibited cytotoxic effects against 12 tested carcinoma cell lines.…”

Section: Diversity Of Hdps Found In the Skin Secretion Of Asian Frmentioning

confidence: 99%

Host Defense Peptides from Asian Frogs as Potential Clinical Therapies

et al. 2015

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Host defense peptides (HDPs) are currently major focal points of medical research as infectious microbes are gaining resistance to existing drugs. They are effective against multi-drug resistant pathogens due to their unique primary target, biological membranes, and their peculiar mode of action. Even though HDPs from 60 Asian frog species belonging to 15 genera have been characterized, research into these peptides is at a very early stage. The purpose of this review is to showcase the status of peptide research in Asia. Here we provide a summary of HDPs from Asian frogs.

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“…However, almost all brevinin-2 peptides possess a net positive charge, a helical conformation, and a unique invariant disulfate loop structure called “ranabox”, consisting of the cyclic Cys-Lys-Xaa-Xaa-Xaa-Xaa-Cys at C-terminus ( Conlon et al, 2009 ; Conlon et al, 2014 ; Savelyeva et al, 2014 ). Brevinin-2 peptides usually show strong antimicrobial activity against gram-negative Escherichia coli and gram-positive Staphylococcus aureus but a relatively low hemolyticity when compared to that of brevinin-1 peptides ( Conlon et al, 2006 ; Conlon et al, 2007 ). Furthermore, brevinin-2GUb at 100 nM has been found to significantly promote insulin release ( Conlon et al, 2008b ).…”

Section: Introductionmentioning

confidence: 99%

Antimicrobial and Anti-inflammatory Effects of a Novel Peptide From the Skin of Frog Microhyla pulchra

et al. 2021

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Brevinins are an important antimicrobial peptide (AMP) family identified in the skin of Ranidae frogs and generally contain a characteristic ranabox structure at their C-terminal sequence. Herein a novel AMP named brevinin-2MP has been identified from the skin of the frog Microhyla pulchra by molecular cloning. Brevinin-2MP (GVITDTLKGVAKTVAAELLRKAHCKLTNSC) with a high amphipathic α-helix in sodium dodecyl sulfate solutions can destroy bacterial cell membrane and kill microbes. Furthermore, brevinin-2MP has been found to inhibit the lipopolysaccharide (LPS)-induced expression of pro-inflammatory NO, MCP-1, IL-6, and TNF-α via binding unidentified targets on the cell membrane and consequently suppressing the activation of MAPK/NF-κB signaling cascades induced by LPS in RAW 264.7 cells. Consistently, brevinin-2MP significantly alleviates the acute inflammatory response in carrageenan-induced mice paw. In conclusion, brevinin-2MP with anti-inflammatory and antimicrobial properties will be an ideal candidate drug molecule for bacterial inflammation treatment.

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Antimicrobial peptides from the skin of the Tsushima brown frog Rana tsushimensis

Cited by 27 publications

References 30 publications

Antimicrobial Peptides from Skin Secretions of Hypsiboas pulchellus (Anura: Hylidae)

Antimicrobial Peptides from Skin Secretions of Hypsiboas pulchellus (Anura: Hylidae)

Host Defense Peptides from Asian Frogs as Potential Clinical Therapies

Antimicrobial and Anti-inflammatory Effects of a Novel Peptide From the Skin of Frog Microhyla pulchra

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