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Two families of antimicrobial peptides with multiple functions from skin of rufous-spotted torrent frog, Amolops loloensis |
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| Authors: | Lu Yi Li Jianxu Yu Haining Xu Xueqing Liang Jianguo Tian Yongqiang Ma Dongying Lin Guoqing Huang Guoqiang Lai Ren |
| Institution: | aKey Laboratory of Microbiological Engineering of Agricultural Environment, Ministry of Agriculture, College of Life Sciences, Nanjing Agricultural University, Nanjing, Jiangsu 210095, China bBiotoxin Units of Key Laboratory of Animal Models and Human Disease Mechanisms, Kunming Institute of Zoology, Chinese Academy of Sciences, Kunming 650223, Yunnan, China cCollege of Life Sciences School of Heibei Normal University, Shijiazhuang, Hebei 050016, China dSchool of Chemical Engineering, Sichuan University, Chengdu 610051, China eGraduate School of the Chinese Academy of Sciences, Beijing 100009, China |
| Abstract: | There are around 27 species of Amolops amphibian distributed in South-east of Asia. Seven antimicrobial peptides (AMPs) belonging to two different families were purified from skin of rufous-spotted torrent frog, Amolops loloensis, and designated brevinins-ALa, b, c, and d, and temporins-ALa, b, and c. The brevinins-AL family which is structurally related to brevinins-1 from skin secretions of the European frog, Rana brevipoda, is composed of 24 amino acids and has an intra-disulfide bridge at the C-terminus. The temporins-AL family, composed of 13 or 16 amino acid residues, is related with temporins from the skin secretions of R. temporaria. The findings of this study will facilitate the solutions to the taxonomic questions of the ranid genus Amolops and Staurois. In the work of this paper, both brevinins-ALb and temporin-Ma induced mast cell degranulation and histamine release, and had cytotoxic activity toward solid tumor cell line HepG2. Brevinins-ALb also exerted strong hemolytic activity while temporin-Ma had no such activity. |
| Keywords: | Amphibian Antimicrobial peptide Diversity Brevinins-AL Temporins-AL Amolops loloensis |
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