Ovchinnikova Tatiana V, Balandin Sergey V, Aleshina Galina M, Tagaev Andrey A, Leonova Yulia F, Krasnodembsky Eugeny D, Men'shenin Alexander V, Kokryakov Vladimir N
Shemyakin and Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, Miklukho-Maklaya str. 16/10, 117997 Moscow, Russia.
Biochem Biophys Res Commun. 2006 Sep 22;348(2):514-23. doi: 10.1016/j.bbrc.2006.07.078. Epub 2006 Jul 28.
A novel 40-residue antimicrobial peptide, aurelin, exhibiting activity against Gram-positive and Gram-negative bacteria, was purified from the mesoglea of a scyphoid jellyfish Aurelia aurita by preparative gel electrophoresis and RP-HPLC. Molecular mass (4296.95 Da) and complete amino acid sequence of aurelin (AACSDRAHGHICESFKSFCKDSGRNGVKLRANCKKTCGLC) were determined. Aurelin has six cysteines forming three disulfide bonds. The total RNA was isolated from the jellyfish mesoglea, RT-PCR and cloning were performed, and cDNA was sequenced. A 84-residue preproaurelin contains a putative signal peptide (22 amino acids) and a propiece of the same size (22 amino acids). Aurelin has no structural homology with any previously identified antimicrobial peptides but reveals partial similarity both with defensins and K+ channel-blocking toxins of sea anemones and belongs to ShKT domain family.
一种新型的40个氨基酸残基的抗菌肽——奥瑞林，对革兰氏阳性菌和革兰氏阴性菌均有活性，通过制备性凝胶电泳和反相高效液相色谱从钵水母纲海月水母的中胶层中纯化得到。测定了奥瑞林的分子量（4296.95道尔顿）和完整氨基酸序列（AACSDRAHGHICESFKSFCKDSGRNGVKLRANCKKTCGLC）。奥瑞林有六个半胱氨酸，形成三个二硫键。从水母中胶层分离出总RNA，进行逆转录聚合酶链反应和克隆，并对cDNA进行测序。一个84个氨基酸残基的前原奥瑞林包含一个推定的信号肽（22个氨基酸）和一个同样大小的前肽（22个氨基酸）。奥瑞林与任何先前鉴定的抗菌肽均无结构同源性，但与防御素以及海葵的钾离子通道阻断毒素均有部分相似性，属于ShKT结构域家族。
