Host defense peptides in skin secretions of the Oregon spotted frog Rana pretiosa: Implications for species resistance to chytridiomycosis

Conlon, J. Michael; Mechkarska, Milena; Ahmed, Eman Farouk; Coquet, Laurent; Jouenne, Thierry; Leprince, Jérôme; Vaudry, Hubert; Hayes, Marc P.; Padgett-Flohr, Gretchen E.

doi:10.1016/j.dci.2011.01.017

Cited by 30 publications

(14 citation statements)

References 48 publications

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“…The first subfamily, the temporin-like subfamily, is represented by 3 peptides, differentiated by an addition of Ala (Dq-1133) and Arg-Ala residues (Dq-1289) in the N-terminal of the sequence and are characterized by a repetitive leucine tail. After APD analyses, these peptides show 46% similarity with temporin K from the European frog Rana temporaria [29] and 43.7% similarity with temporin-CG1 (Amolops chunganensis) [30], Temporin-PRb and Temporin-PRa (Ranapretiosa) [31] and Temporin-SHb (Pelophylax saharica) [32] (Fig. 4A).…”

Section: Discovery Of New Antimicrobial and Antifungal Peptidesmentioning

confidence: 92%

Peptidomic comparison and characterization of the major components of the venom of the giant ant Dinoponera quadriceps collected in four different areas of Brazil

Cologna

Cardoso

Jourdan

et al. 2013

Journal of Proteomics

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Section: Discovery Of New Antimicrobial and Antifungal Peptidesmentioning

confidence: 92%

Peptidomic comparison and characterization of the major components of the venom of the giant ant Dinoponera quadriceps collected in four different areas of Brazil

Cologna

Cardoso

Jourdan

et al. 2013

Journal of Proteomics

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“…It is the first such peptide that inhibits phytopathogenic bacteria [ 20 ]. Hispidalin from winter melon Benincasa hispida [ 34 ] shows only 31% sequence similarity to tachycitin from horseshoe crabs [ 35 ] and amphibian brevinin-1PRb [ 36 ] based on sequence alignment in the APD [ 7 ]. Since hispidalin is a newly discovered peptide, it has not been trained in the existing programs.…”

Section: New Host Defense Peptides Reported In 2014mentioning

confidence: 99%

Antimicrobial Peptides in 2014

et al. 2015

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This article highlights new members, novel mechanisms of action, new functions, and interesting applications of antimicrobial peptides reported in 2014. As of December 2014, over 100 new peptides were registered into the Antimicrobial Peptide Database, increasing the total number of entries to 2493. Unique antimicrobial peptides have been identified from marine bacteria, fungi, and plants. Environmental conditions clearly influence peptide activity or function. Human α-defensin HD-6 is only antimicrobial under reduced conditions. The pH-dependent oligomerization of human cathelicidin LL-37 is linked to double-stranded RNA delivery to endosomes, where the acidic pH triggers the dissociation of the peptide aggregate to release its cargo. Proline-rich peptides, previously known to bind to heat shock proteins, are shown to inhibit protein synthesis. A model antimicrobial peptide is demonstrated to have multiple hits on bacteria, including surface protein delocalization. While cell surface modification to decrease cationic peptide binding is a recognized resistance mechanism for pathogenic bacteria, it is also used as a survival strategy for commensal bacteria. The year 2014 also witnessed continued efforts in exploiting potential applications of antimicrobial peptides. We highlight 3D structure-based design of peptide antimicrobials and vaccines, surface coating, delivery systems, and microbial detection devices involving antimicrobial peptides. The 2014 results also support that combination therapy is preferred over monotherapy in treating biofilms.

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“…Prior to sampling for cutaneous microbes, frogs were rinsed on their dorsal and ventral surfaces by pouring 50 ml of ultrapure water over each surface five times. The final volume of liquid collected was recorded, and peptides were extracted from the water using previously described techniques ( Rollins-Smith et al , 2002 ; Woodhams et al , 2006 ; Sheafor et al , 2008 ; Conlon et al , 2011 ). Briefly, samples were acidified to 1% using trifluoroacetic acid (TFA; Sigma Aldrich, UK) and then passed over individual Sep-Pak C-18 cartridges (Waters Associates, Milford, MA, USA) at a rate of 5 ml/min.…”

Section: Methodsmentioning

confidence: 99%