Effects of glycosylation on antigenicity and immunogenicity of classical swine fever virus envelope proteins
Effects of glycosylation on antigenicity and immunogenicity of classical swine fever virus envelope proteins
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DOI：
10.1016/j.virol.2011.08.025
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发表时间：
2011-11-25
期刊：
影响因子：
3.7
通讯作者：
Risatti, Guillermo R.
中科院分区：
文献类型：
--
作者：
Gavrilov, Boris K.;Rogers, Kara;Risatti, Guillermo R.
猪瘟病毒 (CSFV) 含有三种包膜糖蛋白（E(rns)、E1 和 E2）。先前的研究表明，去除这些蛋白质内的特定糖基化位点会产生减毒且具有免疫原性的 CSFV 突变体。在这里，我们分析了杆状病毒表达的 E(rns)、E1 和 E2 蛋白缺乏糖基化对免疫原性的影响。有趣的是，E(rns)、E1 和 E2 蛋白缺乏适当的翻译后修饰，最明显的是缺乏糖基化，未能诱导可检测的病毒中和抗体 (NA) 反应和针对 CSFV 的保护。同样，在用 E1 糖蛋白免疫的猪中没有观察到 NA 或保护作用。对具有单位点糖基化突变的 E(rns) 和 E2 蛋白的分析表明，特定糖基化位点的去除会影响可检测的抗体反应，但不会影响针对致命性 CSFV 攻击的保护作用。此外，观察到单次施用纯化的E(rns)糖蛋白可诱导针对CSFV感染的有效保护。 (C) 2011 Elsevier Inc. 保留所有权利。
Classical swine fever virus (CSFV) harbors three envelope glycoproteins (E(rns), E1 and E2). Previous studies have demonstrated that removal of specific glycosylation sites within these proteins yielded attenuated and immunogenic CSFV mutants. Here we analyzed the effects of lack of glycosylation of baculovirus-expressed E(rns), E1, and E2 proteins on immunogenicity. Interestingly, E(rns), E1, and E2 proteins lacking proper post-translational modifications, most noticeable lack of glycosylation, failed to induce a detectable virus neutralizing antibody (NA) response and protection against CSFV. Similarly, no NA or protection was observed in pigs immunized with E1 glycoprotein. Analysis of E(rns) and E2 proteins with single site glycosylation mutations revealed that detectable antibody responses, but not protection against lethal CSFV challenge is affected by removal of specific glycosylation sites. In addition, it was observed that single administration of purified E(rns) glycoprotein induced an effective protection against CSFV infection. (C) 2011 Elsevier Inc. All rights reserved.