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天然登革2型病毒蛋白的纯化及纯化蛋白对小鼠的保护能力。

Purification of native dengue-2 viral proteins and the ability of purified proteins to protect mice.

作者信息

Feighny R, Burrous J, McCown J, Hoke C, Putnak R

机构信息

Department of Virus Diseases, Walter Reed Army Institute of Research, Washington, DC.

出版信息

Am J Trop Med Hyg. 1992 Oct;47(4):405-12. doi: 10.4269/ajtmh.1992.47.405.

Abstract

Both the envelope structural protein and the non-structural NS1 protein have been purified from the flavivirus dengue-2 by high-pressure liquid chromatography. These purified proteins maintain their reactivity with monoclonal antibodies. When tested in mice, the envelope protein elicited neutralizing antibodies and partially protected the animals against a lethal viral challenge. The mice responded to the non-structural protein by producing antibodies; however, these antibodies were not neutralizing and the mice were not protected.

摘要

包膜结构蛋白和非结构NS1蛋白均已通过高压液相色谱法从黄病毒登革热2型中纯化出来。这些纯化后的蛋白保持了与单克隆抗体的反应活性。在小鼠实验中,包膜蛋白引发了中和抗体,并部分保护动物免受致命的病毒攻击。小鼠对非结构蛋白产生了抗体反应;然而,这些抗体没有中和作用,小鼠也未得到保护。

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