A family of brevinin-2 peptides with potent activity against Pseudomonas aeruginosa from the skin of the Hokkaido frog, Rana pirica

J. Michael Conlon; Ágnes Sonnevend; Mahrendra Patel; Khawla Al-Dhaheri; Per F. Nielsen; Jolanta Kolodziejek; Norbert Nowotny; Shawichi Iwamuro; Tibor Pál

doi:10.1016/j.regpep.2003.12.003

A family of brevinin-2 peptides with potent activity against Pseudomonas aeruginosa from the skin of the Hokkaido frog, Rana pirica

J. Michael Conlon^*, Ágnes Sonnevend, Mahrendra Patel, Khawla Al-Dhaheri, Per F. Nielsen, Jolanta Kolodziejek, Norbert Nowotny, Shawichi Iwamuro, Tibor Pál

^*Corresponding author for this work

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

57 Citations (Scopus)

Abstract

Nine peptides displaying varying degrees of antimicrobial activity were extracted from the skin of the Hokkaido frog, Rana pirica. Five structurally related peptides were identified as members of the brevinin-2 family. These peptides were active against reference strains of Gram-negative (Escherichia coli, Pseudomonas aeruginosa, Enterobacter cloacae, Klebsiella pneumoniae) and Gram-positive (Staphlococcus aureus) bacteria but displayed relatively low hemolytic activity. The most abundant peptide, brevinin-2PRa (680 nmol/g weight of dry skin) showed high potency [minimal inhibitory concentration (MIC) values between 6 and 12 μM] against a range of clinical isolates of P. aeruginosa. In addition, activity was unaffected by NaCl concentrations up to 200mM. Cladistic analysis based on the primary structures of brevinin-2 peptides supports a close phylogenetic relationship between R. pirica and Japanese mountain brown frog Rana ornativentris. One peptide of the ranatuerin-2 family and one strongly hemolytic peptide of the brevinin-1 family were also isolated from the extract along with two members of the temporin family, temporin-1PRa (ILPILGNLLNGLL.NH₂) and temporin-1PRb (ILPILGNLLNSLL.NH₂) that atypically lacked basic amino acid residues and showed only very weak antimicrobial and hemolytic activity.

Original language	English
Pages (from-to)	135-141
Number of pages	7
Journal	Regulatory Peptides
Volume	118
Issue number	3
DOIs	https://doi.org/10.1016/j.regpep.2003.12.003
Publication status	Published - May 15 2004
Externally published	Yes

Keywords

Antimicrobial
Brevinin-1
Ranatuerin-2
Temporin

ASJC Scopus subject areas

Biochemistry
Physiology
Endocrinology
Clinical Biochemistry
Cellular and Molecular Neuroscience

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10.1016/j.regpep.2003.12.003

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@article{3777e600d2744a01bbe1e871f73e667e,

title = "A family of brevinin-2 peptides with potent activity against Pseudomonas aeruginosa from the skin of the Hokkaido frog, Rana pirica",

abstract = "Nine peptides displaying varying degrees of antimicrobial activity were extracted from the skin of the Hokkaido frog, Rana pirica. Five structurally related peptides were identified as members of the brevinin-2 family. These peptides were active against reference strains of Gram-negative (Escherichia coli, Pseudomonas aeruginosa, Enterobacter cloacae, Klebsiella pneumoniae) and Gram-positive (Staphlococcus aureus) bacteria but displayed relatively low hemolytic activity. The most abundant peptide, brevinin-2PRa (680 nmol/g weight of dry skin) showed high potency [minimal inhibitory concentration (MIC) values between 6 and 12 μM] against a range of clinical isolates of P. aeruginosa. In addition, activity was unaffected by NaCl concentrations up to 200mM. Cladistic analysis based on the primary structures of brevinin-2 peptides supports a close phylogenetic relationship between R. pirica and Japanese mountain brown frog Rana ornativentris. One peptide of the ranatuerin-2 family and one strongly hemolytic peptide of the brevinin-1 family were also isolated from the extract along with two members of the temporin family, temporin-1PRa (ILPILGNLLNGLL.NH2) and temporin-1PRb (ILPILGNLLNSLL.NH2) that atypically lacked basic amino acid residues and showed only very weak antimicrobial and hemolytic activity.",

keywords = "Antimicrobial, Brevinin-1, Ranatuerin-2, Temporin",

author = "Conlon, {J. Michael} and {\'A}gnes Sonnevend and Mahrendra Patel and Khawla Al-Dhaheri and Nielsen, {Per F.} and Jolanta Kolodziejek and Norbert Nowotny and Shawichi Iwamuro and Tibor P{\'a}l",

note = "Funding Information: This work was supported by an Interdisciplinary Grant (03/12-8-03-01) and a Faculty Support Grant (NP/03/01) from the United Arab Emirates University. The authors would like to thank Dr. Farrukh Amin Sheikh, Department of Microbiology, Al-Ain Hospital, UAE for provision of clinical isolates.",

year = "2004",

month = may,

day = "15",

doi = "10.1016/j.regpep.2003.12.003",

language = "English",

volume = "118",

pages = "135--141",

journal = "Regulatory Peptides",

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TY - JOUR

T1 - A family of brevinin-2 peptides with potent activity against Pseudomonas aeruginosa from the skin of the Hokkaido frog, Rana pirica

AU - Conlon, J. Michael

AU - Sonnevend, Ágnes

AU - Patel, Mahrendra

AU - Al-Dhaheri, Khawla

AU - Nielsen, Per F.

AU - Kolodziejek, Jolanta

AU - Nowotny, Norbert

AU - Iwamuro, Shawichi

AU - Pál, Tibor

N1 - Funding Information: This work was supported by an Interdisciplinary Grant (03/12-8-03-01) and a Faculty Support Grant (NP/03/01) from the United Arab Emirates University. The authors would like to thank Dr. Farrukh Amin Sheikh, Department of Microbiology, Al-Ain Hospital, UAE for provision of clinical isolates.

PY - 2004/5/15

Y1 - 2004/5/15

N2 - Nine peptides displaying varying degrees of antimicrobial activity were extracted from the skin of the Hokkaido frog, Rana pirica. Five structurally related peptides were identified as members of the brevinin-2 family. These peptides were active against reference strains of Gram-negative (Escherichia coli, Pseudomonas aeruginosa, Enterobacter cloacae, Klebsiella pneumoniae) and Gram-positive (Staphlococcus aureus) bacteria but displayed relatively low hemolytic activity. The most abundant peptide, brevinin-2PRa (680 nmol/g weight of dry skin) showed high potency [minimal inhibitory concentration (MIC) values between 6 and 12 μM] against a range of clinical isolates of P. aeruginosa. In addition, activity was unaffected by NaCl concentrations up to 200mM. Cladistic analysis based on the primary structures of brevinin-2 peptides supports a close phylogenetic relationship between R. pirica and Japanese mountain brown frog Rana ornativentris. One peptide of the ranatuerin-2 family and one strongly hemolytic peptide of the brevinin-1 family were also isolated from the extract along with two members of the temporin family, temporin-1PRa (ILPILGNLLNGLL.NH2) and temporin-1PRb (ILPILGNLLNSLL.NH2) that atypically lacked basic amino acid residues and showed only very weak antimicrobial and hemolytic activity.

AB - Nine peptides displaying varying degrees of antimicrobial activity were extracted from the skin of the Hokkaido frog, Rana pirica. Five structurally related peptides were identified as members of the brevinin-2 family. These peptides were active against reference strains of Gram-negative (Escherichia coli, Pseudomonas aeruginosa, Enterobacter cloacae, Klebsiella pneumoniae) and Gram-positive (Staphlococcus aureus) bacteria but displayed relatively low hemolytic activity. The most abundant peptide, brevinin-2PRa (680 nmol/g weight of dry skin) showed high potency [minimal inhibitory concentration (MIC) values between 6 and 12 μM] against a range of clinical isolates of P. aeruginosa. In addition, activity was unaffected by NaCl concentrations up to 200mM. Cladistic analysis based on the primary structures of brevinin-2 peptides supports a close phylogenetic relationship between R. pirica and Japanese mountain brown frog Rana ornativentris. One peptide of the ranatuerin-2 family and one strongly hemolytic peptide of the brevinin-1 family were also isolated from the extract along with two members of the temporin family, temporin-1PRa (ILPILGNLLNGLL.NH2) and temporin-1PRb (ILPILGNLLNSLL.NH2) that atypically lacked basic amino acid residues and showed only very weak antimicrobial and hemolytic activity.

KW - Antimicrobial

KW - Brevinin-1

KW - Ranatuerin-2

KW - Temporin

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U2 - 10.1016/j.regpep.2003.12.003

DO - 10.1016/j.regpep.2003.12.003

M3 - Article

C2 - 15003829

AN - SCOPUS:1542289781

SN - 0167-0115

VL - 118

SP - 135

EP - 141

JO - Regulatory Peptides

JF - Regulatory Peptides

IS - 3

ER -

A family of brevinin-2 peptides with potent activity against Pseudomonas aeruginosa from the skin of the Hokkaido frog, Rana pirica

Abstract

Keywords

ASJC Scopus subject areas

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