Komada H, Orstavik I, Ito Y, Norrby E
Department of Virology, Karolinska Institute, School of Medicine, Stockholm, Sweden.
J Gen Virol. 1990 Jul;71 ( Pt 7):1581-3. doi: 10.1099/0022-1317-71-7-1581.
Variations in epitopes on structural proteins of four isolates of parainfluenza virus type 4 (PIV-4) and the Mr of polypeptides in these isolates were determined by radioimmune precipitation assay with monoclonal antibodies to parainfluenza virus type 4A (PIV-4A) and type 4B (PIV-4B). Three isolates antigenically resembled the prototype PIV-4A and the sizes of their structural proteins were 72K (HN protein), 61K (F0 protein), 61K (NP protein) and 40K (M protein). However, one virus isolate showed marked antigenic differences from both the 4A and 4B prototype viruses, particularly with regard to properties of the HN and F proteins. In addition, both the NP and F0 proteins of this isolate had a slightly increased Mr of 63K.
利用抗4A型副流感病毒（PIV-4A）和4B型副流感病毒（PIV-4B）的单克隆抗体，通过放射免疫沉淀试验确定了4株4型副流感病毒（PIV-4）结构蛋白表位的变异情况以及这些病毒株中多肽的相对分子质量。3株病毒在抗原性上与PIV-4A原型相似，其结构蛋白的大小分别为72K（血凝素-神经氨酸酶蛋白）、61K（融合前体蛋白）、61K（核蛋白）和40K（基质蛋白）。然而，有1株病毒分离株与4A和4B原型病毒均表现出明显的抗原差异，尤其是在血凝素-神经氨酸酶蛋白和融合蛋白的特性方面。此外，该分离株的核蛋白和融合前体蛋白的相对分子质量均略有增加，为63K。
