用单克隆抗体研究委内瑞拉马脑脊髓炎减毒病毒的抗原结构。

Biomedical science Pub Date : 1991-01-01
I A Razumov, E V Agapov, A V Pereboev, E V Protopopova, S D Lebedeva, V B Loktev
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引用次数: 0

摘要

利用单克隆抗体对委内瑞拉马脑脊髓炎病毒(VEEV)强毒株和减毒疫苗株的抗原结构进行比较研究,使研究包膜糖蛋白E1和E2的抗原结构成为可能,并明确它们在抗病毒免疫发展中的作用。在E1糖蛋白上有5个由8个表位组成的非重叠抗原位点,可被单克隆抗体识别;在E2糖蛋白上发现6个位点,共20个表位。针对四个位点的单克隆抗体保护动物免受致命的特立尼达驴毒株感染。在确定的负责抗病毒免疫的13个表位中,3个是TC-83菌株的变化,6个属于菌株230的两个位点。所获得的结果表明,有必要进一步改进现有的疫苗制剂,以预防这种危险的传染病。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
Investigation of antigenic structure of attenuated and virulent Venezuelan equine encephalomyelitis virus by means of monoclonal antibodies.

A comparative study of the antigenic structure of virulent strains and attenuated vaccine strains of Venezuelan equine encephalomyelitis virus (VEEV) by means of monoclonal antibodies has made it possible to investigate the antigenic structure of the envelope glycoproteins E1 and E2, and to specify their role in the development of antiviral immunity. On the E1 glycoprotein there are five nonoverlapping antigenic sites consisting of eight epitopes that are recognized by monoclonal antibodies; six sites consisting of twenty epitopes were found on the E2 glycoprotein. The monoclonal antibodies against four sites protect the animals from lethal infection with the virulent strain, Trinidad donkey. Out of the thirteen epitopes identified as being responsible for antiviral immunity, three are changes in the TC-83 strain, and six belong to two sites in the strain 230. The results obtained indicate the necessity for further improvement of the available vaccine preparations against this dangerous infectious disease.

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