TY - JOUR
T1 - Antimicrobial peptides from the skin of the Tsushima brown frog Rana tsushimensis
AU - Conlon, J. Michael
AU - Al-Ghaferi, Nadia
AU - Abraham, Bency
AU - Sonnevend, Agnes
AU - Coquet, Laurent
AU - Leprince, Jérôme
AU - Jouenne, Thierry
AU - Vaudry, Hubert
AU - Iwamuro, Shawichi
N1 - Funding Information:
This work was supported by an Interdisciplinary Grant (03/12-8-03-01) and a Faculty Support Grant (NP/05/01) from the United Arab Emirates University to JMC and by a grant from the Faculty of Science, Toho University to S. I. We wish to thank Mr. Yasushi Midorikawa for the collection of frogs in Tsushima.
PY - 2006/5
Y1 - 2006/5
N2 - The Tsushima brown frog Rana tsushimensis Stejneger, 1907 exists in reproductive isolation on the island of Tsushima, Japan. Six peptides with antimicrobial activity were isolated in pure form from an extract of the skin of this species and their amino acid sequences identified them as members of the brevinin-1 (one peptide), brevinin-2 (one peptide) and temporin (four peptides) families. The C-terminally α-amidated brevinin-1 peptide (FLGSIVGALASALPSLISKIRN.NH2) lacks the cyclic heptapeptide domain Cys18-(Xaa)4-Lys-Cys24 at the COOH-terminus of the molecule that characterizes other members of that family. A structurally similar brevinin-1 peptide, also lacking the cyclic domain, was previously isolated from the skin of the Ryukyu brown frog Rana okinavana, indicative of a close phylogenetic relationship between the species. Brevinin-2TSa (GIMSLFKGVLKTAGKHVAGSLVDQLKCKITGGC) showed broad-spectrum growth inhibitory activity against a range of Gram-negative and Gram-positive bacteria (including methicillin-resistant Staphylococcus aureus) (minimum inhibitory concentrations ≤ 25 μM) and relatively low hemolytic activity against human erythrocytes (LD50 = 100 μM). The peptide therefore represents a candidate for drug development.
AB - The Tsushima brown frog Rana tsushimensis Stejneger, 1907 exists in reproductive isolation on the island of Tsushima, Japan. Six peptides with antimicrobial activity were isolated in pure form from an extract of the skin of this species and their amino acid sequences identified them as members of the brevinin-1 (one peptide), brevinin-2 (one peptide) and temporin (four peptides) families. The C-terminally α-amidated brevinin-1 peptide (FLGSIVGALASALPSLISKIRN.NH2) lacks the cyclic heptapeptide domain Cys18-(Xaa)4-Lys-Cys24 at the COOH-terminus of the molecule that characterizes other members of that family. A structurally similar brevinin-1 peptide, also lacking the cyclic domain, was previously isolated from the skin of the Ryukyu brown frog Rana okinavana, indicative of a close phylogenetic relationship between the species. Brevinin-2TSa (GIMSLFKGVLKTAGKHVAGSLVDQLKCKITGGC) showed broad-spectrum growth inhibitory activity against a range of Gram-negative and Gram-positive bacteria (including methicillin-resistant Staphylococcus aureus) (minimum inhibitory concentrations ≤ 25 μM) and relatively low hemolytic activity against human erythrocytes (LD50 = 100 μM). The peptide therefore represents a candidate for drug development.
KW - Antimicrobial peptide
KW - Brevinin-1
KW - Brevinin-2
KW - Frog skin
KW - HPLC purification
KW - Temporin
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U2 - 10.1016/j.cbpc.2005.11.022
DO - 10.1016/j.cbpc.2005.11.022
M3 - Article
C2 - 16413829
AN - SCOPUS:33645418011
SN - 1532-0456
VL - 143
SP - 42
EP - 49
JO - Comparative Biochemistry and Physiology - C Toxicology and Pharmacology
JF - Comparative Biochemistry and Physiology - C Toxicology and Pharmacology
IS - 1
ER -