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使用单克隆抗体分析17D黄热病毒包膜蛋白表位

Analysis of 17D yellow fever virus envelope protein epitopes using monoclonal antibodies.

作者信息

Schlesinger J J, Walsh E E, Brandriss M W

出版信息

J Gen Virol. 1984 Oct;65 ( Pt 10):1637-44. doi: 10.1099/0022-1317-65-10-1637.

Abstract

Sixteen monoclonal antibodies that reacted with the envelope glycoprotein (E) of 17D vaccine strain yellow fever virus (17D YF), including two antibodies produced against dengue 2 virus, were used in a solid phase competitive binding assay (CBA) to define spatial relationships among antigenic determinants on 17D YF E. The antibodies showed YF strain, type or flavivirus group specificities and nine epitopes were identified on 17D YF E by patterns of neutralization, haemagglutination inhibition and competition of antibody binding. Epitopes defined by neutralizing antibodies with strain and type specificities appeared spatially distant but competition between type-specific neutralizing antibodies and some non-neutralizing antibodies against type and group determinants suggested close proximity among epitopes in these regions. Despite competition between some neutralizing and non-neutralizing monoclonal antibodies in CBA, plaque assays revealed no interference with neutralization by non-neutralizing antibody.

摘要

16种与17D疫苗株黄热病毒(17D YF)包膜糖蛋白(E)发生反应的单克隆抗体,包括两种针对登革2病毒产生的抗体,被用于固相竞争结合试验(CBA),以确定17D YF E上抗原决定簇之间的空间关系。这些抗体表现出黄热病毒株、型或黄病毒属特异性,通过中和、血凝抑制和抗体结合竞争模式在17D YF E上鉴定出9个表位。由具有株和型特异性的中和抗体定义的表位在空间上似乎相距较远,但型特异性中和抗体与一些针对型和属决定簇的非中和抗体之间的竞争表明这些区域的表位彼此接近。尽管在CBA中一些中和与非中和单克隆抗体之间存在竞争,但蚀斑试验显示非中和抗体对中和作用没有干扰。

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