A melittin-related peptide from the skin of the Japanese frog, Rana tagoi, with antimicrobial and cytolytic properties

J. Michael Conlon; Agnes Sonnevend; Mahendra Patel; Vijayayasarathy Camasamudram; Norbert Nowotny; Erika Zilahi; Shawichi Iwamuro; Per F. Nielsen; Tibor Pál

doi:10.1016/S0006-291X(03)00999-9

A melittin-related peptide from the skin of the Japanese frog, Rana tagoi, with antimicrobial and cytolytic properties

J. Michael Conlon^*, Agnes Sonnevend, Mahendra Patel, Vijayayasarathy Camasamudram, Norbert Nowotny, Erika Zilahi, Shawichi Iwamuro, Per F. Nielsen, Tibor Pál

^*Corresponding author for this work

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

60 Citations (Scopus)

Abstract

Two peptides with antimicrobial and cytolytic properties were purified from an extract of the skin of Tago's brown frog Rana tagoi. The primary structure of one peptide (FLPILGKLLS¹⁰GIL·NH₂) identifies it as a member of the temporin family, whereas the second peptide (AIGSILGALA¹⁰KGLPTLISWI²⁰KNR·NH₂) displays 78% sequence identity to melittin from the venom of the honeybee Apis florea. Compared with melittin, the melittin-related peptide (MRP) was equipotent in inhibiting the growth of the Gram-positive bacterium Staphylococcus aureus, 5-fold less potent against the Gram-negative bacterium Escherichia coli and against the fungal pathogen, Candida albicans. MRP was 13-fold less hemolytic than melittin against human erythrocytes and 4- and 5-fold less cytolytic against mouse EL4 T-lymphoma-derived cells and L929 fibroblasts, respectively. However, at non-cytotoxic concentrations (≤8μM), MRP did not protect HeLa cells from cell death produced by human rhinovirus type 2 infection.

Original language	English
Pages (from-to)	496-500
Number of pages	5
Journal	Biochemical and Biophysical Research Communications
Volume	306
Issue number	2
DOIs	https://doi.org/10.1016/S0006-291X(03)00999-9
Publication status	Published - Jun 27 2003
Externally published	Yes

Keywords

Antimicrobial
Antiviral
Cytolytic
Frog skin
Hemolytic
Melittin
Temporin

ASJC Scopus subject areas

Biophysics
Biochemistry
Molecular Biology
Cell Biology

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10.1016/S0006-291X(03)00999-9

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@article{bb183f3a7cee420ea5ad8c3abea942cc,

title = "A melittin-related peptide from the skin of the Japanese frog, Rana tagoi, with antimicrobial and cytolytic properties",

abstract = "Two peptides with antimicrobial and cytolytic properties were purified from an extract of the skin of Tago's brown frog Rana tagoi. The primary structure of one peptide (FLPILGKLLS10GIL·NH2) identifies it as a member of the temporin family, whereas the second peptide (AIGSILGALA10KGLPTLISWI20KNR·NH2) displays 78% sequence identity to melittin from the venom of the honeybee Apis florea. Compared with melittin, the melittin-related peptide (MRP) was equipotent in inhibiting the growth of the Gram-positive bacterium Staphylococcus aureus, 5-fold less potent against the Gram-negative bacterium Escherichia coli and against the fungal pathogen, Candida albicans. MRP was 13-fold less hemolytic than melittin against human erythrocytes and 4- and 5-fold less cytolytic against mouse EL4 T-lymphoma-derived cells and L929 fibroblasts, respectively. However, at non-cytotoxic concentrations (≤8μM), MRP did not protect HeLa cells from cell death produced by human rhinovirus type 2 infection.",

keywords = "Antimicrobial, Antiviral, Cytolytic, Frog skin, Hemolytic, Melittin, Temporin",

author = "Conlon, {J. Michael} and Agnes Sonnevend and Mahendra Patel and Vijayayasarathy Camasamudram and Norbert Nowotny and Erika Zilahi and Shawichi Iwamuro and Nielsen, {Per F.} 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 thank Prof. D. Blaas, Institute of Medical Biochemistry, University of Vienna and Prof. T. Popow-Kraupp, Institute of Virology, University of Vienna for providing viruses and HeLa cells.",

year = "2003",

month = jun,

day = "27",

doi = "10.1016/S0006-291X(03)00999-9",

language = "English",

volume = "306",

pages = "496--500",

journal = "Biochemical and Biophysical Research Communications",

issn = "0006-291X",

publisher = "Academic Press Inc.",

number = "2",

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TY - JOUR

T1 - A melittin-related peptide from the skin of the Japanese frog, Rana tagoi, with antimicrobial and cytolytic properties

AU - Conlon, J. Michael

AU - Sonnevend, Agnes

AU - Patel, Mahendra

AU - Camasamudram, Vijayayasarathy

AU - Nowotny, Norbert

AU - Zilahi, Erika

AU - Iwamuro, Shawichi

AU - Nielsen, Per F.

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 thank Prof. D. Blaas, Institute of Medical Biochemistry, University of Vienna and Prof. T. Popow-Kraupp, Institute of Virology, University of Vienna for providing viruses and HeLa cells.

PY - 2003/6/27

Y1 - 2003/6/27

N2 - Two peptides with antimicrobial and cytolytic properties were purified from an extract of the skin of Tago's brown frog Rana tagoi. The primary structure of one peptide (FLPILGKLLS10GIL·NH2) identifies it as a member of the temporin family, whereas the second peptide (AIGSILGALA10KGLPTLISWI20KNR·NH2) displays 78% sequence identity to melittin from the venom of the honeybee Apis florea. Compared with melittin, the melittin-related peptide (MRP) was equipotent in inhibiting the growth of the Gram-positive bacterium Staphylococcus aureus, 5-fold less potent against the Gram-negative bacterium Escherichia coli and against the fungal pathogen, Candida albicans. MRP was 13-fold less hemolytic than melittin against human erythrocytes and 4- and 5-fold less cytolytic against mouse EL4 T-lymphoma-derived cells and L929 fibroblasts, respectively. However, at non-cytotoxic concentrations (≤8μM), MRP did not protect HeLa cells from cell death produced by human rhinovirus type 2 infection.

AB - Two peptides with antimicrobial and cytolytic properties were purified from an extract of the skin of Tago's brown frog Rana tagoi. The primary structure of one peptide (FLPILGKLLS10GIL·NH2) identifies it as a member of the temporin family, whereas the second peptide (AIGSILGALA10KGLPTLISWI20KNR·NH2) displays 78% sequence identity to melittin from the venom of the honeybee Apis florea. Compared with melittin, the melittin-related peptide (MRP) was equipotent in inhibiting the growth of the Gram-positive bacterium Staphylococcus aureus, 5-fold less potent against the Gram-negative bacterium Escherichia coli and against the fungal pathogen, Candida albicans. MRP was 13-fold less hemolytic than melittin against human erythrocytes and 4- and 5-fold less cytolytic against mouse EL4 T-lymphoma-derived cells and L929 fibroblasts, respectively. However, at non-cytotoxic concentrations (≤8μM), MRP did not protect HeLa cells from cell death produced by human rhinovirus type 2 infection.

KW - Antimicrobial

KW - Antiviral

KW - Cytolytic

KW - Frog skin

KW - Hemolytic

KW - Melittin

KW - Temporin

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U2 - 10.1016/S0006-291X(03)00999-9

DO - 10.1016/S0006-291X(03)00999-9

M3 - Article

C2 - 12804591

AN - SCOPUS:0038546578

VL - 306

SP - 496

EP - 500

JO - Biochemical and Biophysical Research Communications

JF - Biochemical and Biophysical Research Communications

SN - 0006-291X

IS - 2

ER -

A melittin-related peptide from the skin of the Japanese frog, Rana tagoi, with antimicrobial and cytolytic properties

Abstract

Keywords

ASJC Scopus subject areas

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