title: Novel antimicrobial peptides isolated from the skin secretions of Hainan odorous frog, Odorrana hainanensis.
abstract: Long time geographical isolation of Hainan Island from the China continent has resulted in appearance of many novel frog species. As one of them, Hainan odorous frog, Odorrana hainanensis possesses some special antimicrobial peptides distinct from those found in other Odorrana. In this study, three antimicrobial peptides have been purified and characterized from the skin secretion of O. hainanensis. With the similarity to the temporin family, two peptides are characterized by amidated C-terminals, so they are named as temporin-HN1 (AILTTLANWARKFL-NH(2)) and temporin-HN2 (NILNTIINLAKKIL-NH(2)). The third antimicrobial peptide belongs to the brevinin-1 family which is widely distributed in Eurasian ranids, and thus, it is named as brevinin-1HN1 (FLPLIASLAANFVPKIFCKITKKC). Furthermore, after sequencing 68 clones, eight cDNAs encoding antimicrobial peptide precursors were cloned from the skin-derived cDNA library of O. hainanensis. These eight cDNAs can encode seven mature antimicrobial peptides including the above three, as well as brevinin-1V, brevinin-2HS2, odorranain-A6, and odorranain-B1. Twelve different species of microorganisms were chosen, including Gram-positive, Gram-negative and fungi, to test the antimicrobial activities of temporin-HN1, temporin-HN2, brevinin-1HN1, brevinin-1V, and brevinin-2HS2. The result shows that, in addition to their activities against Gram-positive bacteria, temporin-HN1 and temporin-HN2 also possess activities against some Gram-negative bacteria and fungi. However, the two antimicrobial peptides, brevinin-1HN1 and brevinin-1V of the brevinin-1 family have stronger antimicrobial activities than temporin-HN1 and temporin-HN2 of the temporin family. Brevinin-1HN1 possesses activity against Staphylococcus aureus (ATCC25923), Rhodococcus rhodochrous X15, and Slime mould 090223 at the concentration of 1.2 μM.
authors.affiliation: Key Laboratory of Animal Physiology, Biochemistry and Molecular Biology of Hebei Province, College of Life Sciences, Hebei Normal University, Shijiazhuang, Hebei, China.
authors.forename: Hui
authors.initials: H
authors.lastname: Wang
authors.forename: Zhijun
authors.initials: Z
authors.lastname: Yu
authors.forename: Yuhong
authors.initials: Y
authors.lastname: Hu
authors.forename: Fengjiao
authors.initials: F
authors.lastname: Li
authors.forename: Limeng
authors.initials: L
authors.lastname: Liu
authors.forename: Hongyuan
authors.initials: H
authors.lastname: Zheng
authors.forename: Hao
authors.initials: H
authors.lastname: Meng
authors.forename: Shujie
authors.initials: S
authors.lastname: Yang
authors.forename: Xiaolong
authors.initials: X
authors.lastname: Yang
authors.forename: Jingze
authors.initials: J
authors.lastname: Liu
mesh_terms: D000595:Amino Acid Sequence; D029845:Amphibian Proteins / Q000737:chemistry / Q000302:isolation & purification / Q000494:pharmacology*; D000818:Animals; D000890:Anti-Infective Agents / Q000737:chemistry / Q000302:isolation & purification / Q000494:pharmacology; D023181:Antimicrobial Cationic Peptides / Q000737:chemistry / Q000302:isolation & purification / Q000494:pharmacology*; D005260:Female; D005658:Fungi / Q000187:drug effects*; D006090:Gram-Negative Bacteria / Q000187:drug effects*; D006094:Gram-Positive Bacteria / Q000187:drug effects*; D008297:Male; D008826:Microbial Sensitivity Tests; D017433:Protein Structure, Secondary; D011506:Proteins / Q000302:isolation & purification / Q000494:pharmacology; D011898:Ranidae / Q000378:metabolism*; D012867:Skin / Q000378:metabolism
chemical_list: D029845:Amphibian Proteins; D000890:Anti-Infective Agents; D023181:Antimicrobial Cationic Peptides; D011506:Proteins; C530453:odorranain-NR, Odorrana grahami; C104501:temporin; C078413:brevinin-1 protein, Rana