Isolation and characterisation of oncorhyncin II, a histone H1-derived antimicrobial peptide from skin secretions of rainbow trout, Oncorhynchus mykiss
Isolation and characterisation of oncorhyncin II, a histone H1-derived antimicrobial peptide from skin secretions of rainbow trout, Oncorhynchus mykiss
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DOI：
10.1016/s0145-305x(03)00120-4
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发表时间：
2004-02-01
影响因子：
2.9
通讯作者：
Smith, VJ
中科院分区：
文献类型：
--
作者：
Fernandes, JMO;Molle, G;Smith, VJ
从虹鳟鱼皮肤分泌物的酸提取物中分离出一种有效的抗菌肽，暂命名为oncorhyncin II。氨基酸测序结果表明，oncorhyncin II的前17个残基与虹鳟组蛋白H1的138 ~ 154个残基相同。基质辅助激光解吸电离质谱分析表明，纯化肽的分子量为7195.3 Da。综上所述，这些数据表明oncorhyncin II是组蛋白H1的69个残基c端片段，可能在两个残基上被磷酸化。在亚微摩尔范围内，Oncorhyncin II对革兰氏-(+)和革兰氏-(-)细菌具有最低的抑制浓度，对鳟鱼红细胞没有显着的溶血活性。纯化的肽被发现可以诱导平面脂质双分子层的明显不稳定，而不形成稳定的离子通道。Oncorhyncin II可能是组蛋白H1的裂解产物，在虹鳟鱼的粘膜防御中具有潜在的重要作用。(C) 2003 Elsevier Ltd.版权所有。
A potent antimicrobial peptide, tentatively named oncorhyncin II, was isolated from an acid extract of rainbow trout skin secretions. Amino acid sequencing showed that the first 17 residues of oncorhyncin II are identical to residues 138-154 of histone H1 from rainbow trout. Matrix-assisted laser desorption ionization mass spectrometry revealed that the purified peptide has a molecular mass of 7195.3 Da. Taken together, these data indicate that oncorhyncin II is a 69-residue C-terminal fragment of histone H1, probably phosphorylated at two residues. Oncorhyncin II has minimal inhibitory concentrations in the submicromolar range against Gram-(+) as well as Gram-(-) bacteria and it does not display significant haemolytic activity towards trout erythrocytes. The purified peptide was found to induce a marked destabilisation of planar lipid bilayers without the formation of stable ion channels. Oncorhyncin II is possibly a cleavage product of histone H1 with a potentially important role in mucosal defence of rainbow trout. (C) 2003 Elsevier Ltd. All rights reserved.