Stable secretion of a soluble, oligomeric form of rabies virus glycoprotein: influence of N-glycan processing on secretion.
Stable secretion of a soluble, oligomeric form of rabies virus glycoprotein: influence of N-glycan processing on secretion.
复制标题
狂犬病病毒糖蛋白可溶性寡聚形式的稳定分泌：N-聚糖加工对分泌的影响。
DOI：
10.1021/bi00008a026
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发表时间：
1995
期刊：
影响因子：
2.9
通讯作者：
Spitalnik,SL
中科院分区：
文献类型：
--
作者：
Wojczyk,B;Shakin-Eshleman,SH;Doms,RW;Xiang,ZQ;Ertl,HC;Wunner,WH;Spitalnik,SL
狂犬病病毒糖蛋白（RGP）是一种由505个氨基酸组成的I型跨膜糖蛋白，在狂犬病病毒感染的发病机制中起重要作用。RGP还刺激宿主产生中和抗体。N-连接糖基化是RGP细胞表面表达和免疫原性所必需的。在当前的研究中，通过在跨膜结构域外部插入终止密码子构建的可溶形式的RGP在转染的中国仓鼠卵巢细胞中表达。发现RGP的可溶形式具有适当的抗原性和免疫原性。与全长RGP类似，可溶性形式组装成同源二聚体和同源三聚体。可溶性RGP的分泌和全长RGP的细胞表面表达需要核心糖基化。此外，A-聚糖的初始葡萄糖修剪对于可溶性RGP的分泌和全长RGP的细胞表面表达是必要的和足够的。来自Evelyn-Rokitnicki-Abelseth（ERA）毒株的狂犬病病毒糖蛋白（RGP）1是505个氨基酸的I型膜糖蛋白，其含有22个氨基酸的跨膜结构域和44个氨基酸的胞质结构域（Fishbein和罗宾逊，1993; Wunner等人，1988年）。胞外结构域具有三个潜在的N-连接的gly-
Revised Manuscript Received December 6, 1994® abstract: Rabies virus glycoprotein (RGP) is a 505 amino acid type I transmembrane glycoprotein that is important in the pathogenesis of rabies virus infection. RGPalso stimulates the development of neutralizing antibodies by the host. N-Linked glycosylation is required for both cell surface expression and immunogenicity of RGP. In the current study, a soluble form of RGP, constructed by insertion of a stop codon external to the transmembrane domain, was expressed in transfectedChinese hamster ovary cells. The soluble form of RGP was found to be appropriately antigenic and immunogenic. Similar to full-length RGP, the soluble form was assembled into homodimers and homotrimers. Core glycosylation was required for secretion of soluble RGP and cell surface expression of full-length RGP. In addition, initial glucose trimming of the A-glycans was necessary and sufficient for secretion of soluble RGP and cell surface expression of full-length RGP. Further iV-glycan processing was not required for secretion or cell surface expression of soluble or full-length RGP, respectively.Rabies virusglycoprotein (RGP) 1 from the Evelyn—Rokitnicki-Abelseth (ERA) strain is a 505 amino acid type I membrane glycoprotein containing a 22 amino acid transmembrane domain and a 44 amino acid cytoplasmic domain (Fishbein & Robinson, 1993; Wunner et al., 1988). The extracellular domain has three potential N-linked gly-