中国仓鼠卵巢细胞
免疫原性
生物
重组DNA
糖蛋白
分子生物学
病毒学
抗体
糖基化
蛋白质亚单位
病毒
细胞培养
融合蛋白
生物化学
基因
免疫学
遗传学
作者
Michèle Haumont,Alain Jacquet,Marc Massaer,Virginie Deleersnyder,Pasqualina Mazzu,Alex Bollen,Paul Jacobs
出处
期刊:Virus Research
[Elsevier]
日期:1996-02-01
卷期号:40 (2): 199-204
被引量:40
标识
DOI:10.1016/0168-1702(95)01270-2
摘要
The gene of the varicella-zoster virus (VZV) glycoprotein gE, engineered to code for a truncated molecule lacking the anchor and carboxy-terminal tail domains, was transfected into Chinese hamster ovary (CHO) cells via the pEE14 mammalian expression vector. One recombinant cell line, CHO-gE-2–9, secreted high levels of truncated gE into the culture medium. The product was purified to near homogeneity by a combination of anion exchange, hydrophobic and metal-chelate chromatographies. Purified recombinant gE showed the expected amino-terminal sequence and its glycosylation pattern proved similar to that of the natural product. When injected into mice, using either Freund's or alum as adjuvant, the native truncated gE induced complement-dependent neutralizing antibodies. In contrast, when the molecule was first denatured, it lost immunogenicity with alum. These data show that the recombinant gE, although truncated, could potentially be included in a subunit vaccine against VZV infection.
科研通智能强力驱动
Strongly Powered by AbleSci AI