Matheise J P, Walravens K, Collard A, Coppe P, Letesson J J
Laboratoire de Microbiologie-Immunologie, Facultés Universitaires Notre-Dame de la Paix, Namur, Belgium.
Arch Virol. 1995;140(6):993-1005. doi: 10.1007/BF01315410.
From two independent fusions, fifteen MAbs directed to the F protein of the bovine respiratory syncytial virus (BRSV) were characterized by radio-immunoprecipitation assays. Competition binding assays among these MAbs identified two distinct antigenic sites (A and B) and one overlapping site (AB). All of the MAbs specific to epitopes belonging to site A neutralized the infectivity of the virus in vitro and recognized human and bovine RSV strains. Only two out of the five MAbs directed to epitopes of site B were neutralizing and three reacted with all of the RSV strains tested, suggesting that the epitopes constituting this domain present heterogeneous characteristics. In each of sites A and B, one of the neutralizing MAbs also inhibited cell fusion. The biological relevance of these domains was established by competing representative MAbs and sera from BRSV-infected calves.
通过两种独立的融合方法，利用放射免疫沉淀试验对15种针对牛呼吸道合胞病毒（BRSV）F蛋白的单克隆抗体（MAb）进行了特性鉴定。这些单克隆抗体之间的竞争结合试验确定了两个不同的抗原位点（A和B）和一个重叠位点（AB）。所有针对位点A表位的单克隆抗体在体外均能中和病毒的感染性，并能识别人类和牛呼吸道合胞病毒株。针对位点B表位的5种单克隆抗体中只有2种具有中和作用，3种与所有测试的呼吸道合胞病毒株发生反应，这表明构成该结构域的表位具有异质性特征。在A和B位点中，各有一个具有中和作用的单克隆抗体也能抑制细胞融合。通过竞争来自感染BRSV的犊牛的代表性单克隆抗体和血清，确定了这些结构域的生物学相关性。
