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猪nectin-1的第一个免疫球蛋白样结构域足以使转基因小鼠对伪狂犬病病毒感染产生抗性。

The first immunoglobulin-like domain of porcine nectin-1 is sufficient to confer resistance to pseudorabies virus infection in transgenic mice.

作者信息

Ono E, Tomioka Y, Watanabe Y, Amagai K, Taharaguchi S, Glenisson J, Cherel P

机构信息

The Avian Zoonoses Research Centre, Faculty of Agriculture, Tottori University, Tottori, Japan.

出版信息

Arch Virol. 2006 Sep;151(9):1827-39. doi: 10.1007/s00705-006-0747-6. Epub 2006 Apr 3.

DOI:10.1007/s00705-006-0747-6
PMID:16583156
Abstract

Nectin-1 is an alphaherpesvirus receptor that binds to virion glycoprotein D (gD). Porcine nectin-1 mediates entry of pseudorabies virus (PRV), herpes simplex virus types 1 and 2 (HSV-1 and HSV-2), and bovine herpesvirus type 1 (BHV-1). The gD-binding domain of nectin-1 is the first or N-terminal immunoglobulin (Ig)-like domain of the entire ectodomain. Here, we generated three transgenic mouse lines expressing a fusion protein consisting of the first Ig-like domain of porcine nectin-1 and the Fc portion of porcine IgG1 to assess the antiviral potential of the first Ig-like domain of nectin-1 in vivo. All of the transgenic mouse lines showed significant resistance to PRV infection via intraperitoneal inoculation (survival rates of 67% to 100%). In the intranasal challenge, a lower but still significant protection was observed; 21% to 55% of the animals from the three transgenic mouse lines survived. The present results demonstrate that a soluble form of the first domain of porcine nectin-1 is able to exert a significant antiviral effect against pseudorabies virus infection.

摘要

Nectin-1是一种与病毒粒子糖蛋白D(gD)结合的α疱疹病毒受体。猪Nectin-1介导伪狂犬病病毒(PRV)、1型和2型单纯疱疹病毒(HSV-1和HSV-2)以及1型牛疱疹病毒(BHV-1)的进入。Nectin-1的gD结合结构域是整个胞外结构域的第一个或N端免疫球蛋白(Ig)样结构域。在此,我们构建了三个表达由猪Nectin-1的第一个Ig样结构域和猪IgG1的Fc部分组成的融合蛋白的转基因小鼠品系,以评估Nectin-1的第一个Ig样结构域在体内的抗病毒潜力。所有转基因小鼠品系经腹腔接种后对PRV感染均表现出显著抗性(存活率为67%至100%)。在鼻内攻毒实验中观察到较低但仍显著的保护作用;三个转基因小鼠品系中有21%至55%的动物存活。目前的结果表明,猪Nectin-1第一个结构域的可溶性形式能够对伪狂犬病病毒感染发挥显著的抗病毒作用。

相似文献

1
The first immunoglobulin-like domain of porcine nectin-1 is sufficient to confer resistance to pseudorabies virus infection in transgenic mice.猪nectin-1的第一个免疫球蛋白样结构域足以使转基因小鼠对伪狂犬病病毒感染产生抗性。
Arch Virol. 2006 Sep;151(9):1827-39. doi: 10.1007/s00705-006-0747-6. Epub 2006 Apr 3.
2
Fusion protein consisting of the first immunoglobulin-like domain of porcine nectin-1 and Fc portion of human IgG1 provides a marked resistance against pseudorabies virus infection to transgenic mice.由猪nectin-1的第一个免疫球蛋白样结构域和人IgG1的Fc部分组成的融合蛋白为转基因小鼠提供了对伪狂犬病病毒感染的显著抗性。
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Transgenic mice expressing a soluble form of porcine nectin-1/herpesvirus entry mediator C as a model for pseudorabies-resistant livestock.表达可溶性形式的猪nectin-1/疱疹病毒进入介质C的转基因小鼠作为抗伪狂犬病家畜的模型。
Proc Natl Acad Sci U S A. 2004 Nov 16;101(46):16150-5. doi: 10.1073/pnas.0405816101. Epub 2004 Nov 8.
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Use of chimeric nectin-1(HveC)-related receptors to demonstrate that ability to bind alphaherpesvirus gD is not necessarily sufficient for viral entry.利用嵌合的nectin-1(HveC)相关受体来证明,与α疱疹病毒gD结合的能力不一定足以实现病毒进入。
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Glycoprotein D homologs in herpes simplex virus type 1, pseudorabies virus, and bovine herpes virus type 1 bind directly to human HveC(nectin-1) with different affinities.单纯疱疹病毒1型、伪狂犬病病毒和牛疱疹病毒1型中的糖蛋白D同源物以不同亲和力直接与人HveC(nectin-1)结合。
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Enhanced resistance to herpes simplex virus type 1 infection in transgenic mice expressing a soluble form of herpesvirus entry mediator.表达可溶性形式疱疹病毒进入介质的转基因小鼠对1型单纯疱疹病毒感染的抗性增强
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Resistance to pseudorabies virus infection in transgenic mice expressing the chimeric transgene that represses the immediate-early gene transcription.表达抑制立即早期基因转录的嵌合转基因的转基因小鼠对伪狂犬病病毒感染的抗性
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Comparison of the antiviral potentials among the pseudorabies-resistant transgenes encoding different soluble forms of porcine nectin-1 in transgenic mice.转基因小鼠中编码不同可溶性形式猪nectin-1的伪狂犬病抗性转基因之间抗病毒潜力的比较。
J Gen Virol. 2007 Oct;88(Pt 10):2636-2641. doi: 10.1099/vir.0.83080-0.
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Porcine HveC, a member of the highly conserved HveC/nectin 1 family, is a functional alphaherpesvirus receptor.猪HveC是高度保守的HveC/nectin 1家族的成员,是一种功能性α疱疹病毒受体。
Virology. 2001 Mar 15;281(2):315-28. doi: 10.1006/viro.2000.0798.

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