Characterization of diverse antimicrobial peptides in skin secretions of Chungan torrent frog Amolops chunganensis

• Published in: Peptides (New York, N.Y. : 1980) Vol. 38; no. 1; pp. 41 - 53
• Main Authors: Yang, Xiaohong, Xia, Jiangnan, Yu, Zhijun, Hu, Yuhong, Li, Fengjiao, Meng, Hao, Yang, Shujie, Liu, Jingze, Wang, Hui
• Format: Journal Article
• Language: English
• Published: United States Elsevier Inc 01.11.2012
• Subjects: Amino Acid Sequence; amino acid sequences; Amolops; Amolops chunganensis; Amphibian; Amphibian Proteins - genetics; Amphibian Proteins - isolation & purification; Amphibian Proteins - pharmacology; Animals; Anti-Infective Agents - chemistry; Anti-Infective Agents - pharmacology; anti-infective properties; Antimicrobial Cationic Peptides - genetics; Antimicrobial peptides; Anura; Bodily Secretions - chemistry; cDNA libraries; Cloning, Molecular; complementary DNA; erythrocytes; Erythrocytes - drug effects; Frog skin; frogs; fungi; Gram-negative bacteria; Gram-Negative Bacteria - drug effects; Gram-positive bacteria; Gram-Positive Bacteria - drug effects; hemolysis; Hemolytic Agents - pharmacology; Humans; Microbial Sensitivity Tests; Molecular Sequence Data; Phylogeny; Proteins - genetics; Ranidae; Rhodococcus rhodochrous; sequence analysis; Skin - chemistry; Amolops chunganensis; Frog skin; Amphibian; Antimicrobial peptides
• ISSN: 0196-9781; 1873-5169
• DOI: 10.1016/j.peptides.2012.08.008

► cDNAs encoding 11 antimicrobial peptides were cloned. ► Seven antimicrobial peptides were first purified from skin secretions of Amolops chunganensis. ► Effects of antimicrobial peptides on microorganism and human erythrocytes were observed by SEM. ► Phylogenetic analysis of A. chunganensis based upon the primary structures of brevinin-1, brevinin-2, and esculentin-2 families antimicrobial peptides. We have cloned, synthesized, and characterized 11 novel antimicrobial peptides from a skin derived cDNA library of the Chungan torrent frog, Amolops chunganensis. Seven of the 11 antimicrobial peptides were present in authentic A. chunganensis skin secretions. Sequence analysis indicated that the 11 peptides belonged to the temporin, esculentin-2, palustrin-2, brevinin-1, and brevinin-2 families. The peptides displayed potent antimicrobial activities against several strains of microorganisms. One peptide, brevinin-1CG5, demonstrated antimicrobial activity against all tested Gram-positive and Gram-negative bacteria and fungi, and showed high antimicrobial potency (MIC=0.6μM) against Gram-positive bacterium Rhodococcus rhodochrous. Some peptides also demonstrated weak hemolytic activity against human erythrocytes in vitro. Phylogenetic analysis based on the amino acid sequences of brevinin-1, brevinin-2, and esculentin-2 peptides from family Ranidae confirmed that the current taxonomic status of A. chunganensis is correct.