Role of the N-linked glycans of the prM and E envelope proteins in tick-borne encephalitis virus particle secretion

Role of the N-linked glycans of the prM and E envelope proteins in tick-borne encephalitis virus particle secretion
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DOI:
10.1016/j.vaccine.2004.11.068
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发表时间:
2005-04-27
期刊:
影响因子:
5.5
通讯作者:
Takashima, I
Takashima, I
中科院分区:
医学3区
文献类型:
--
作者:
Goto, A;Yoshii, K;Takashima, I

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森林脑炎(TBE)病毒有两种膜糖蛋白(PrM和E),每种糖蛋白都有一个N-连接的糖蛋白。表达TBE病毒PRM和E蛋白的构建物已被证明能产生病毒样颗粒(VLP),其表面特性类似于传染性病毒。为了揭示TBE病毒PrM和E蛋白糖基化在VLP分泌中的作用,我们表达了糖基化突变的PrM和E蛋白,并对VLP的分泌水平和生物学特性进行了比较。在PrM蛋白糖基化缺陷突变体中,分泌的E蛋白水平下降到野生型的60%0。另一方面,在E或PrM-E蛋白糖基化缺陷突变体中,E蛋白的分泌水平下降到野生型的10%。此外,在E蛋白的66和154位糖基化的突变体分泌的E蛋白水平是野生型的4倍。然而,在仅在第66位糖基化的突变体中,E蛋白的分泌仅减少到野生型水平的10%。这些数据表明,与蛋白E第154位N-连接糖基化位点相关的多糖在VLP的分泌中起着重要作用。(C)2004爱思唯尔有限公司。保留所有权利。
The tick-borne encephalitis (TBE) virus has two membrane glycoproteins (prM and E), which each has one N-linked glycan. Constructs that express prM and E proteins of TBE virus have been shown to produce virus-like particles (VLPs), which have surface properties that are similar to those of infectious viruses. To reveal the function of glycosylation of the TBE virus prM and E proteins in the secretion of VLPs, we expressed glycosylation-mutated prM and E proteins and compared the secretion levels and biological properties of the VLPs. In the prM protein glycosylation-deficient mutant, the level of secreted E protein was reduced to 60%0 of the wild-type level. On the other hand, in the E or prM-E protein glycosylation-deficient mutant, the level of secreted E protein was reduced to 10% of the wild-type level. Furthermore, the mutant which was glycosylated at positions 66 and 154 in protein E, the level of secreted E protein was four-fold higher than that of the wild-type. However, in the mutant which was glycosylated at position 66 only, E protein secretion was reduced to only 10% of the wild-type level. These data suggest that the glycan associated with the N-linked glycosylation site at position 154 in protein E plays an important role in VLP secretion. (c) 2004 Elsevier Ltd. All rights reserved.