Yusoff K, Nesbit M, McCartney H, Meulemans G, Alexander D J, Collins M S, Emmerson P T, Samson A C
Department of Biochemistry and Genetics, Medical School, University of Newcastle upon Tyne, U.K.
J Gen Virol. 1989 Nov;70 ( Pt 11):3105-9. doi: 10.1099/0022-1317-70-11-3105.
A panel of eight neutralizing monoclonal antibodies (MAbs) against the fusion (F) protein of Newcastle disease virus (NDV) has been shown to locate a major antigenic site on the basis of competitive binding assay and additivity index studies. Five epitopes (A1 to A5) have been located within this site on the F protein of the Beaudette C strain of NDV on the basis of cross-resistance plaque assays of MAb-resistant mutants raised against these MAbs. Epitopes A1, A4 and A5 are distinct; epitope A2 partially overlaps epitope A3. Nucleotide sequence analysis of the F genes of MAb-resistant mutants showed that each predicted single amino acid substitutions ranging from amino acid residues 157 to 171 for epitope A4 and at residues 72, 78, 79 and 343 for epitopes A1, A2, A3 and A5 respectively. These locations indicate that both the F1 and F2 fragments are involved in the formation of a single antigenic site and suggest the involvement of extensive protein folding in the active form of this F protein.
一组针对新城疫病毒(NDV)融合(F)蛋白的八种中和单克隆抗体(MAb)已通过竞争性结合试验和加和指数研究确定了一个主要抗原位点。基于针对这些单克隆抗体产生的抗单克隆抗体突变体的交叉抗性蚀斑试验,在NDV博德特C株F蛋白的该位点内定位了五个表位(A1至A5)。表位A1、A4和A5是不同的;表位A2部分重叠表位A3。抗单克隆抗体突变体F基因的核苷酸序列分析表明,每个预测的单个氨基酸取代分别对应表位A4的157至171位氨基酸残基以及表位A1、A2、A3和A5的72、78、79和343位残基。这些位置表明F1和F2片段都参与了单个抗原位点的形成,并提示广泛的蛋白质折叠参与了该F蛋白活性形式的形成。