Wojczyk B, Shakin-Eshleman S H, Doms R W, Xiang Z Q, Ertl H C, Wunner W H, Spitalnik S L
Department of Pathology, University of Pennsylvania School of Medicine, Philadelphia 19104.
Biochemistry. 1995 Feb 28;34(8):2599-609. doi: 10.1021/bi00008a026.
Rabies virus glycoprotein (RGP) is a 505 amino acid type I transmembrane glycoprotein that is important in the pathogenesis of rabies virus infection. RGP also 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 transfected Chinese 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 N-glycans was necessary and sufficient for secretion of soluble RGP and cell surface expression of full-length RGP. Further N-glycan processing was not required for secretion or cell surface expression of soluble or full-length RGP, respectively.
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还能刺激宿主产生中和抗体。N-糖基化对于RGP的细胞表面表达和免疫原性均是必需的。在本研究中，通过在跨膜结构域外插入一个终止密码子构建的可溶性RGP形式，在转染的中国仓鼠卵巢细胞中表达。可溶性RGP被发现具有适当的抗原性和免疫原性。与全长RGP相似，可溶性形式组装成同源二聚体和同源三聚体。核心糖基化对于可溶性RGP的分泌和全长RGP的细胞表面表达是必需的。此外，N-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且充分的。可溶性或全长RGP的分泌或细胞表面表达分别不需要进一步的N-聚糖加工。
