Open AccessTemporins, Antimicrobial Peptides from the European Red Frog Rana temporaria
Author(s) -
Simmaco Maurizio,
Mignogna Giuseppina,
Canofeni Silvia,
Miele Rossella,
Mangoni Maria Luisa,
Barra Donatella
Publication year - 1996
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1996.0788r.x
Subject(s) - complementary dna , signal peptide , peptide , cdna library , biology , antimicrobial peptides , peptide sequence , microbiology and biotechnology , rana , frog skin , biochemistry , chemistry , gene , anatomy , organic chemistry , sodium
A cDNA library from the skin of Rana temporaria has been screened using a cDNA fragment probe that encodes the signal peptide of the precursor of esculentin from the skin secretion of Rana esculentu. With this approach, the cDNAs encoding the precursors of three peptides were isolated. Subsequently, the peptides predicted from the sequence of the cloned cDNAs as well as several structurally related peptides could be isolated from the skin secretion of R. temporuria. These peptides, which were named temporins, have a length of 10–13 residues and show some sequence similarity to hemolytic peptides isolated from Vespu venom [Argiolas, A. & Pisano, J. J. (1984) J. Biol. Chem. 259 , 10106–10111]. Natural and synthetic temporins have antibacterial activity against gram‐positive bacteria, but they are not hemolytic. Temporins are the smallest antibacterial peptides hitherto found in nature.