Antimicrobial peptides from the skin secretions of the South-East Asian frog Hylarana erythraea (Ranidae)

Nadia Al-Ghaferi; Jolanta Kolodziejek; Norbert Nowotny; Laurent Coquet; Thierry Jouenne; Jérôme Leprince; Hubert Vaudry; Jay D. King; J. Michael Conlon

doi:10.1016/j.peptides.2009.12.013

Antimicrobial peptides from the skin secretions of the South-East Asian frog Hylarana erythraea (Ranidae)

Nadia Al-Ghaferi, Jolanta Kolodziejek, Norbert Nowotny, Laurent Coquet, Thierry Jouenne, Jérôme Leprince, Hubert Vaudry, Jay D. King, J. Michael Conlon^*

^*Corresponding author for this work

Research output: Contribution to journal › Article › peer-review

33 Citations (Scopus)

Abstract

Peptidomic analysis of norepinephrine-stimulated skin secretions of the South-East Asian frog Hylarana erythraea (formerly Rana erythraea partim) has led to the identification of multiple peptides with antimicrobial activity. Structural characterization of the peptides demonstrated that they belong to the brevinin-1 (3), brevinin-2 (2), esculentin-2 (4), and temporin (1) families. The values in parentheses indicate the number of paralogs. In addition, a peptide (GVIKSVLKGVAKTVALG ML.NH₂) was isolated that shows some structural similarity to the brevinin-2-related peptides (B2RP) previously isolated from North American frogs of the genus Lithobates. A synthetic replicate of the species B2RP showed broad-spectrum growth inhibitory activity against reference strains of Escherichia coli (MIC = 12.5 μM), Staphylococcus aureus (MIC = 12.5 μM) and Candida albicans (MIC = 50 μM) and was active against multidrug-resistant clinical isolates of Acetinobacter baumannii (MIC in the range 6-12.5 μM). The hemolytic activity of the peptide was relatively low (LC₅₀ = 280 μM). Phylogenetic analysis based upon the amino acid sequences of 47 brevinin-2 peptides from 17 Asian species belonging to the family Ranidae provides support for the placement of H. erythraea in the genus Hylarana.

Original language	English
Pages (from-to)	548-554
Number of pages	7
Journal	Peptides
Volume	31
Issue number	4
DOIs	https://doi.org/10.1016/j.peptides.2009.12.013
Publication status	Published - Apr 2010
Externally published	Yes

Keywords

Antimicrobial peptide
Brevinin
Esculentin-2
Frog skin
Hylarana
Temporin

ASJC Scopus subject areas

Biochemistry
Physiology
Endocrinology
Cellular and Molecular Neuroscience

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10.1016/j.peptides.2009.12.013

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@article{59faa4d720944702868a45bf260c07ff,

title = "Antimicrobial peptides from the skin secretions of the South-East Asian frog Hylarana erythraea (Ranidae)",

abstract = "Peptidomic analysis of norepinephrine-stimulated skin secretions of the South-East Asian frog Hylarana erythraea (formerly Rana erythraea partim) has led to the identification of multiple peptides with antimicrobial activity. Structural characterization of the peptides demonstrated that they belong to the brevinin-1 (3), brevinin-2 (2), esculentin-2 (4), and temporin (1) families. The values in parentheses indicate the number of paralogs. In addition, a peptide (GVIKSVLKGVAKTVALG ML.NH2) was isolated that shows some structural similarity to the brevinin-2-related peptides (B2RP) previously isolated from North American frogs of the genus Lithobates. A synthetic replicate of the species B2RP showed broad-spectrum growth inhibitory activity against reference strains of Escherichia coli (MIC = 12.5 μM), Staphylococcus aureus (MIC = 12.5 μM) and Candida albicans (MIC = 50 μM) and was active against multidrug-resistant clinical isolates of Acetinobacter baumannii (MIC in the range 6-12.5 μM). The hemolytic activity of the peptide was relatively low (LC50 = 280 μM). Phylogenetic analysis based upon the amino acid sequences of 47 brevinin-2 peptides from 17 Asian species belonging to the family Ranidae provides support for the placement of H. erythraea in the genus Hylarana.",

keywords = "Antimicrobial peptide, Brevinin, Esculentin-2, Frog skin, Hylarana, Temporin",

author = "Nadia Al-Ghaferi and Jolanta Kolodziejek and Norbert Nowotny and Laurent Coquet and Thierry Jouenne and J{\'e}r{\^o}me Leprince and Hubert Vaudry and King, {Jay D.} and Conlon, {J. Michael}",

note = "Funding Information: This work was supported by an Interdisciplinary Grant (01-03-2-12/08) and a Faculty Support Grant from U.A.E. University. The authors thank Tibor Pal and Agnes Sonnevend, Department of Medical Microbiology, UAE University for supply of bacterial strains and help with the microbiological assays. ",

year = "2010",

month = apr,

doi = "10.1016/j.peptides.2009.12.013",

language = "English",

volume = "31",

pages = "548--554",

journal = "Peptides",

issn = "0196-9781",

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T1 - Antimicrobial peptides from the skin secretions of the South-East Asian frog Hylarana erythraea (Ranidae)

AU - Al-Ghaferi, Nadia

AU - Kolodziejek, Jolanta

AU - Nowotny, Norbert

AU - Coquet, Laurent

AU - Jouenne, Thierry

AU - Leprince, Jérôme

AU - Vaudry, Hubert

AU - King, Jay D.

AU - Conlon, J. Michael

N1 - Funding Information: This work was supported by an Interdisciplinary Grant (01-03-2-12/08) and a Faculty Support Grant from U.A.E. University. The authors thank Tibor Pal and Agnes Sonnevend, Department of Medical Microbiology, UAE University for supply of bacterial strains and help with the microbiological assays.

PY - 2010/4

Y1 - 2010/4

N2 - Peptidomic analysis of norepinephrine-stimulated skin secretions of the South-East Asian frog Hylarana erythraea (formerly Rana erythraea partim) has led to the identification of multiple peptides with antimicrobial activity. Structural characterization of the peptides demonstrated that they belong to the brevinin-1 (3), brevinin-2 (2), esculentin-2 (4), and temporin (1) families. The values in parentheses indicate the number of paralogs. In addition, a peptide (GVIKSVLKGVAKTVALG ML.NH2) was isolated that shows some structural similarity to the brevinin-2-related peptides (B2RP) previously isolated from North American frogs of the genus Lithobates. A synthetic replicate of the species B2RP showed broad-spectrum growth inhibitory activity against reference strains of Escherichia coli (MIC = 12.5 μM), Staphylococcus aureus (MIC = 12.5 μM) and Candida albicans (MIC = 50 μM) and was active against multidrug-resistant clinical isolates of Acetinobacter baumannii (MIC in the range 6-12.5 μM). The hemolytic activity of the peptide was relatively low (LC50 = 280 μM). Phylogenetic analysis based upon the amino acid sequences of 47 brevinin-2 peptides from 17 Asian species belonging to the family Ranidae provides support for the placement of H. erythraea in the genus Hylarana.

AB - Peptidomic analysis of norepinephrine-stimulated skin secretions of the South-East Asian frog Hylarana erythraea (formerly Rana erythraea partim) has led to the identification of multiple peptides with antimicrobial activity. Structural characterization of the peptides demonstrated that they belong to the brevinin-1 (3), brevinin-2 (2), esculentin-2 (4), and temporin (1) families. The values in parentheses indicate the number of paralogs. In addition, a peptide (GVIKSVLKGVAKTVALG ML.NH2) was isolated that shows some structural similarity to the brevinin-2-related peptides (B2RP) previously isolated from North American frogs of the genus Lithobates. A synthetic replicate of the species B2RP showed broad-spectrum growth inhibitory activity against reference strains of Escherichia coli (MIC = 12.5 μM), Staphylococcus aureus (MIC = 12.5 μM) and Candida albicans (MIC = 50 μM) and was active against multidrug-resistant clinical isolates of Acetinobacter baumannii (MIC in the range 6-12.5 μM). The hemolytic activity of the peptide was relatively low (LC50 = 280 μM). Phylogenetic analysis based upon the amino acid sequences of 47 brevinin-2 peptides from 17 Asian species belonging to the family Ranidae provides support for the placement of H. erythraea in the genus Hylarana.

KW - Antimicrobial peptide

KW - Brevinin

KW - Esculentin-2

KW - Frog skin

KW - Hylarana

KW - Temporin

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DO - 10.1016/j.peptides.2009.12.013

M3 - Article

C2 - 20015460

AN - SCOPUS:77649236303

SN - 0196-9781

VL - 31

SP - 548

EP - 554

JO - Peptides

JF - Peptides

IS - 4

ER -

Antimicrobial peptides from the skin secretions of the South-East Asian frog Hylarana erythraea (Ranidae)

Abstract

Keywords

ASJC Scopus subject areas

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