cDNA cloning of three cecropin‐like antimicrobial peptides (Styelins) from the tunicate, Styela clava

FEBS Letters

Lee, In Hee¹  Liaw, Lilian¹  Zhao, Chengquan¹  Lehrer, Robert I¹ 

[1] Department of Medicine, UCLA School of Medicine, Los Angeles, CA 90095-1690, USA

关键词: Antimicrobial peptide;    cDNA;    Cecropin;    Styelin;    Styela clava;    Tunicate;   

DOI  :  10.1016/S0014-5793(97)00769-2

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

We cloned precursors of three new antimicrobial peptides, Styelins C, D and E, from a pharyngeal cDNA library of a tunicate, Styela clava. Preprostyelins resembled dipteran preprocecropins, while the mature domain of Styelin C resembled Cecropin P1, an antimicrobial peptide purified from the porcine intestine. Beginning with the last 6 residues of their signal sequences, Styelin C and Cecropin 1 from Drosophila virilis had 8/11 identical amino acids (72.7%). Moreover, 4 of the last 6 residues of their mature peptide domains were also identical. Styelins were shorter, by 8 residues, than dipteran cecropins and preprostyelins contained a conserved, polyanionic C-terminal extension that was absent in preprocecropins. Delineation of cecropin-like antimicrobial peptides in a protochordate supports the antiquity of this family as effectors of innate immunity in animals and it increases the likelihood that additional cecropin-like peptides will be found among other evolutionary descendants of protochordates — vertebrates.

【 授权许可】

Unknown