Acanthoscurrin:: a novel glycine-rich antimicrobial peptide constitutively expressed in the hemocytes of the spider Acanthoscurria gomesiana
Acanthoscurrin:: a novel glycine-rich antimicrobial peptide constitutively expressed in the hemocytes of the spider Acanthoscurria gomesiana
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DOI：
10.1016/s0145-305x(03)00058-2
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发表时间：
2003-10-01
影响因子：
2.9
通讯作者：
Daffre, S
中科院分区：
文献类型：
--
作者：
Lorenzini, DM;da Silva, PI;Daffre, S
我们报告从未受挑战的狼蛛 Acanthoscurria gomesiana 的血细胞中分离出一种新型抗菌肽，即棘皮素。 Edman 降解、质谱分析和 cDNA 克隆相结合，揭示了棘菔素的两种亚型的存在，其差异在于两个甘氨酸残基。两者都显示出阳离子特性和高比例的甘氨酸残基。然而，棘菔素与已知的来自动物和植物的富含甘氨酸的抗菌肽没有结构相似性。根据 cDNA 克隆和质谱分析推论，棘蝽素的氨基酸序列以 23 个氨基酸的推定信号肽开始，随后是成熟肽，该成熟肽通过 C 末端酰胺化进行翻译后修饰。棘红素在血细胞中组成型表达，并在免疫攻击后释放到血浆中。 (C) 2003 Elsevier Science Ltd. 保留所有权利。
We report the isolation of a novel antimicrobial peptide, acanthoscurrin, from the hemocytes of unchallenged tarantula spider Acanthoscurria gomesiana. A combination of Edman degradation, mass spectrometry and cDNA cloning revealed the presence of two isoforms of acanthoscurrin, differing by two glycine residues. Both displayed cationic properties and a high percentage of glycine residues. However, acanthoscurrins have no structural similarities with already known glycine-rich antimicrobial peptides from animals and plants. As deduced from cDNA cloning and mass spectrometry, the amino acid sequence of acanthoscurrin begins with a putative signal peptide of 23 amino acids followed by the mature peptide, which is post-translationally modified by a C-terminal amidation. Acanthoscurrins are constitutively expressed in hemocytes and released to plasma following an immune challenge. (C) 2003 Elsevier Science Ltd. All rights reserved.