Leonov S V, Utter G, Waris M, Norrby E
Microbiology and Tumorbiology Centre, Karolinska Institute, Solma, Stockholm, Sweden.
J Gen Virol. 1994 Jun;75 ( Pt 6):1353-9. doi: 10.1099/0022-1317-75-6-1353.
Three linear antigenic regions on the P protein from human respiratory syncytial virus (RSV) subgroup A (strain A2) were represented by peptides that reacted with monoclonal antibodies and with sera from humans with recent or previous RSV infection. The determinants were localized within three hydrophilic regions of the P protein: Pro91 to Asp110, Ser161 to Lys180 and Glu221 to Phe241. The role of individual amino acids in the epitopes defined by monoclonal antibodies was determined. Two monoclonal antibodies reacting with the same antigenic site were found to detect epitopes that had different amino acid dependencies. Rabbit hyperimmune sera raised against selected peptides specifically precipitated different forms of the P protein from RSV-infected 35S-labelled cell extracts in a radioimmune precipitation assay. These findings have implications for forthcoming structural-functional studies of RSV capsid component interactions and also for serological diagnosis of RSV infection.
人呼吸道合胞病毒（RSV）A亚组（A2株）P蛋白上的三个线性抗原区域由与单克隆抗体以及近期或既往感染过RSV的人的血清发生反应的肽段所代表。这些决定簇定位于P蛋白的三个亲水区内：Pro91至Asp110、Ser161至Lys180以及Glu221至Phe241。确定了单克隆抗体所定义表位中单个氨基酸的作用。发现两种与相同抗原位点发生反应的单克隆抗体可检测具有不同氨基酸依赖性的表位。在放射免疫沉淀试验中，针对选定肽段产生的兔超免疫血清可从RSV感染的35S标记细胞提取物中特异性沉淀出不同形式的P蛋白。这些发现对即将开展的RSV衣壳成分相互作用的结构功能研究以及RSV感染的血清学诊断具有重要意义。
