Differences in signal peptide processing between GP3 glycoproteins of Arteriviridae.
Differences in signal peptide processing between GP3 glycoproteins of Arteriviridae.
复制标题
DOI：
10.1016/j.virol.2017.11.026
复制
发表时间：
2017-12
期刊：
影响因子：
3.7
通讯作者：
Minze Zhang;M. Veit
中科院分区：
文献类型：
--
作者：
Minze Zhang;M. Veit
我们以前曾报道，马动脉炎病毒(EAV)的GP3信号肽附近的一个重叠的糖基化位点上的碳水化合物可以防止切割。在这里，我们调查了这种不寻常的处理方案是否是其他动脉病毒科的GP3的一个特征，这些GP3都在相似的位置包含一个糖基化位点。猪繁殖与呼吸综合征病毒(PRRSV)和乳酸脱氢酶提升病毒(LDV)的GP3表达表明，GP3使用了第一糖基化位点，但对信号肽的切割没有影响。将PRRSV和LDV脱糖后的GP3与含信号肽和不含信号肽的突变体进行比较，结果表明GP3的S信号肽已被切割。在EAV和PRRSV的GP3之间交换信号肽发现，共翻译处理的信息不是在信号肽中编码的，而是在GP3的其余部分中编码的。
We reported previously that carbohydrate attachment to an overlapping glycosylation site adjacent to the signal peptide of GP3 from equine arteritis virus (EAV) prevents cleavage. Here we investigated whether this unusual processing scheme is a feature of GP3s of otherArteriviridae, which all contain a glycosylation site at a similar position. Expression of GP3 from type-1 and type-2 porcine reproductive and respiratory syndrome virus (PRRSV) and from lactate dehydrogenase-elevating virus (LDV) revealed that the first glycosylation site is used, but has no effect on signal peptide cleavage. Comparison of the SDS-PAGE mobility of deglycosylated GP3 from PRRSV and LDV with mutants having or not having a signal peptide showed that GP3´s signal peptide is cleaved. Swapping the signal peptides between GP3 of EAV and PRRSV revealed that the information for co-translational processing is not encoded in the signal peptide, but in the remaining part of GP3.