Giansanti Francesco, Massucci M Teresa, Giardi M Federica, Nozza Fabrizio, Pulsinelli Emy, Nicolini Claudio, Botti Dario, Antonini Giovanni
Department of Biology, University of Roma TRE, I-00154 Roma, Italy.
Biochem Biophys Res Commun. 2005 May 27;331(1):69-73. doi: 10.1016/j.bbrc.2005.03.125.
Ovotransferrin and lactoferrin are iron-binding proteins with antiviral and antibacterial activities related to natural immunity, showing marked sequence and structural homologies. The antiviral activity of two hen ovotransferrin fragments DQKDEYELL (hOtrf(219-227)) and KDLLFK (hOtrf(269-301) and hOtrf(633-638)) towards Marek's disease virus infection of chicken embryo fibroblasts is reported here. These fragments have sequence homology with two bovine lactoferrin fragments with antiviral activity towards herpes simplex virus, suggesting that these fragments could have a role for the exploitation of the antiviral activity of the intact proteins towards herpes viruses. NMR analysis showed that these peptides, chemically synthetized, did not possess any favourite conformation in solution, indicating that both the aminoacid sequence and the conformation they display in the intact protein are essential for the antiviral activity.
卵转铁蛋白和乳铁蛋白是具有与天然免疫相关的抗病毒和抗菌活性的铁结合蛋白,显示出明显的序列和结构同源性。本文报道了两种鸡卵转铁蛋白片段DQKDEYELL(hOtrf(219 - 227))和KDLLFK(hOtrf(269 - 301)和hOtrf(633 - 638))对鸡胚成纤维细胞马立克氏病病毒感染的抗病毒活性。这些片段与两种对单纯疱疹病毒具有抗病毒活性的牛乳铁蛋白片段具有序列同源性,表明这些片段可能在利用完整蛋白质对疱疹病毒的抗病毒活性方面发挥作用。核磁共振分析表明,这些化学合成的肽在溶液中不具有任何优势构象,这表明氨基酸序列及其在完整蛋白质中呈现的构象对于抗病毒活性都是必不可少的。