Ranatuerins: Antimicrobial Peptides Isolated from the Skin of the American Bullfrog,Rana catesbeiana

Goraya, Jadvinder; Knoop, Floyd C.; Conlon, J. Michael

doi:10.1006/bbrc.1998.9362

Cited by 123 publications

(52 citation statements)

References 18 publications

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“…In addition, PIs appear to be a class of drugs representing a vital source of lead compounds for the treating or preventing of infection by viruses or pathogens, including HIV and Hepatitis C, in accordance with their capability of inhibiting the extracellular proteases which are believed to be widely produced by many pathogens (Christeller 2005). Thus PIs are useful tools to study and ultimately to better understand the functional principles of protein actives leading to the design of highly-specific drugs to control pathologic processes (Dockray et al 1975, Sampaio et al 1996, Goraya et al 1998.…”

Section: Introductionmentioning

confidence: 99%

“…Kunitz inhibitors have been found in the skin secretions of bombinid toads and ranid frogs, Kazal inhibitors in phyllomedusine frogs and Bowman-Birk inhibitors in ranid frogs. Kunitz protease inhibitors usually contain four Cys residues that form two disulphide bridges and a single reactive centre as canonical structural features of the group [4,](Conlon et al 2009, Sampaio et al 1996, Goraya et al 1998. Furthermore, Kunitz-type inhibitors containing the rare signal peptide disulphide bridges have been isolated from frog skin secretions and this new type of trypsin inhibitor is apparently widely present in these secretions such that it can provide a wide spectrum of action templates for designing specific inhibitors for discrete protease targets (Lambert et al 2004).…”

Section: Introductionmentioning

confidence: 99%

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Kunitzins: Prototypes of a new class of protease inhibitor from the skin secretions of European and Asian frogs

Chen

Wang

Shen

et al. 2016

Biochemical and Biophysical Research Communications

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Amphibian skin secretions contain biologically-active compounds, such as antimicrobial peptides and trypsin inhibitors, which are used by biomedical researchers as a source of potential novel drug leads or pharmacological agents. Here, we report the application of a recently developed technique within our laboratory to "shotgun" clone the cDNAs encoding two novel but structurally-related peptides from the lyophilized skin secretions of one species of European frog, Rana esculentaand one species of Chinese frog, Odorranaschmackeri. Bioanalysis of the peptides established the structure of a 17-mer with an N-terminal Ala (A) residue and a C-terminal Cys (C) residue with a single disulphide bridge between Cys 12 and 17, which is a canonical Kunitz-type protease inhibitor motif (-CKAAFC-). Due to the presence of this structural attribute, these peptides were named kunitzin-RE (AAKIILNPKFRCKAAFC) and kunitzin-OS (AVNIPFKVHLRCKAAFC).Synthetic replicates of these two novel peptides were found to display a potent inhibitory activity against Escherichia coli but were ineffective at inhibiting the growth of Staphylococcus aureus and Candida albicans at concentrations up to 160μM and both showed little haemolytic activity at concentrations up to 120μM. Subsequently, kunitzin-RE and kunitzin-OSwere found to be a potent inhibitor of trypsin with a Ki of 5.56 µM and 7.56µM that represent prototypes of a novel class of highly-attenuated amphibian skin protease inhibitor. Substitution of Lys-13, the predicted residue occupying the P1 position within the inhibitory loop, with Phe (F) resulted in decrease in trypsin inhibitor effectiveness and antimicrobial activity against Esherichia coli, but exhibits a potential inhibition activity against chymotrysin.

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Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Kunitzins: Prototypes of a new class of protease inhibitor from the skin secretions of European and Asian frogs

Chen

Wang

Shen

et al. 2016

Biochemical and Biophysical Research Communications

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“…Our results suggest that the effect of pH should be taken into consideration in all assays of antimicrobial peptides. Staphylococcus aureus is also inhibited by peptides from plethodontid salamanders (Fredericks and Dankert, 2000) and several frog species (Zasloff, 1987;Goraya et al, 1998Goraya et al, , 2000Matutte et al, 2000;Conlon et al, 2004). Klebsiella pneumoniae was shown to be inhibited by Magainin 2, a peptide from Xenopus laevis (Zasloff, 1987).…”

Section: Discussionmentioning

confidence: 98%

Antimicrobial Peptide Defenses in the Salamander, Ambystoma Tigrinum, Against Emerging Amphibian Pathogens

Sheafor

Davidson

Parr

et al. 2008

Journal of Wildlife Diseases

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ABSTRACT:Skin peptides were collected from living Ambystoma tigrinum larvae and adults and tested against two emerging pathogens, Batrachochytrium dendrobatidis and the Ambystoma tigrinum virus (ATV), as well as bacteria isolated from A. tigrinum. Natural mixtures of skin peptides were found to inhibit growth of B. dendrobatidis, Staphylococcus aureus, and Klebsiella sp., but activity against ATV was unpredictable. Skin peptides collected from salamanders held at three environmentally relevant temperatures differed in activity against B. dendrobatidis. Activity of the A. tigrinum skin peptides was found to be strongly influenced by pH.

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“…Magainins (16), ranatuerin-2, temporin families (63,64) and dermaseptins (25) adopt an amphipathic a-helial conformation, either in aqueous solution or upon interaction with membranes of microorganisms (64). However, ranatuerin-1, aurein 1.2 and caerin 1.1 from Australian frog adopt random coil arrangement in aqueous solution and an a-helical structure in membrane mimetic environments (65)(66)(67)(68)(69).…”

Section: Secondary Structure Of Antimicrobial Peptidesmentioning

confidence: 99%

“…Increasing positive charge of AMP is a strategy to improve antimicrobial potency. Ranatuerin-1 (SMLSVLKNLG 10 KVGLGFVACK 20 INKQC) isolated from the skin of the bullfrog R. catesbeiana contains broad-spectrum antimicrobial activity (63). Substitution of Lys to Asn 8 increased positive charge and potency (between 2-fold and 8-fold) against tested strains (S. aureus, P. aeruginosa and C. albicans) with only a very small increase in hemolytic activity (130).…”

Section: Modification Of Chargementioning

confidence: 99%

Antimicrobial peptides from amphibians

Xiao

Liu

Lai

2011

BioMolecular Concepts

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Increased prevalence of multi-drug resistance in pathogens has encouraged researchers to focus on finding novel forms of anti-infective agents. Antimicrobial peptides (AMPs) found in animal secretions are components of host innate immune response and have survived eons of pathogen evolution. Thus, they are likely to be active against pathogens and even those that are resistant to conventional drugs. Many peptides have been isolated and shown to be effective against multi-drug resistant pathogens. More than 500 AMPs have been identified from amphibians. The abundance of AMPs in frog skin is remarkable and constitutes a rich source for design of novel pharmaceutical molecules. Expression and post-translational modifications, discovery, activities and probable therapeutic application prospects of amphibian AMPs will be discussed in this article.

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Ranatuerins: Antimicrobial Peptides Isolated from the Skin of the American Bullfrog,Rana catesbeiana

Cited by 123 publications

References 18 publications

Kunitzins: Prototypes of a new class of protease inhibitor from the skin secretions of European and Asian frogs

Kunitzins: Prototypes of a new class of protease inhibitor from the skin secretions of European and Asian frogs

Antimicrobial Peptide Defenses in the Salamander, Ambystoma Tigrinum, Against Emerging Amphibian Pathogens

Antimicrobial peptides from amphibians

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