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

*المؤلف المقابل لهذا العمل

نتاج البحث: المساهمة في مجلةمراجعة النظراء

53 اقتباسات (Scopus)

ملخص

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.

اللغة الأصليةEnglish
الصفحات (من إلى)135-141
عدد الصفحات7
دوريةRegulatory Peptides
مستوى الصوت118
رقم الإصدار3
المعرِّفات الرقمية للأشياء
حالة النشرPublished - مايو 15 2004
منشور خارجيًانعم

ASJC Scopus subject areas

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