Involvement of bovine lactoferrin metal saturation, sialic acid and protein fragments in the inhibition of rotavirus infection
Involvement of bovine lactoferrin metal saturation, sialic acid and protein fragments in the inhibition of rotavirus infection
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DOI：
10.1016/s0304-4165(01)00178-7
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发表时间：
2001-10-03
影响因子：
3
通讯作者：
Antonini, G
中科院分区：
文献类型：
--
作者：
Superti, F;Siciliano, R;Antonini, G
虽然乳铁蛋白的抗病毒活性是这种铁结合蛋白的主要生物学功能之一，但其作用机制仍存在争议。我们研究了金属结合，唾液酸和牛乳铁蛋白（bLf）的胰蛋白酶片段对轮状病毒（肠道病原体裸病毒）感染肠细胞样细胞的活性的作用。与脱辅基或铁饱和的bLf相比，锰或锌完全饱和的bLf的抗病毒活性略有降低。不同金属饱和的bLf对轮状病毒的抗病毒活性在病毒附着步骤期间和之后发挥。唾液酸的去除增强了bLf的抗轮状病毒活性。在通过胰蛋白酶消化bLf获得并通过高级质谱方法表征的所有肽片段中，大片段（86-258）和小肽（324-329：YLTTLK）能够抑制轮状病毒，即使在比未消化的bLf更低的程度上。(C)2001 Elsevier Science B. V.保留所有权利。
Although the antiviral activity of lactoferrin is one of the major biological functions of this iron binding protein, the mechanism of action is still under debate. We have investigated the role of metal binding, of sialic acid and of tryptic fragments of bovine lactoferrin (bLf) in the activity towards rotavirus (intestinal pathogen naked virus) infecting enterocyte-like cells. The antiviral activity of bLf fully saturated with manganese or zinc was slightly decreased compared to that observed for apo- or iron-saturated bLf. The antiviral activity of differently metal-saturated bLf towards rotavirus was exerted during and after the virus attachment step. The removal of sialic acid enhanced the antirotavirus activity of bLf. Among all the peptidic fragments obtained by tryptic digestion of bLf and characterised by advanced mass spectrometric methodologies, a large fragment (86-258) and a small peptide (324-329: YLTTLK) were able to inhibit rotavirus even if at lower extent than undigested bLf. (C) 2001 Elsevier Science B.V. All rights reserved.