A family of brevinin-2 peptides with potent activity against Pseudomonas aeruginosa from the skin of the Hokkaido frog, Rana pirica
A family of brevinin-2 peptides with potent activity against Pseudomonas aeruginosa from the skin of the Hokkaido frog, Rana pirica
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DOI:
10.1016/j.regpep.2003.12.003
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发表时间:
2004-05-15
影响因子:
--
通讯作者:
Pál, T
中科院分区:
文献类型:
--
作者:
Conlon, JM;Sonnevend, A;Pál, T
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 muM] 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. (C) 2004 Elsevier B.V. All rights reserved.