Andrés G, Simón-Mateo C, Viñuela E
Centro de Biología Molecular (C.S.I.C.-U.A.M.), Facultad de Ciencias, Universidad Autónoma, Cantoblancó, Madrid, Spain.
Virology. 1993 May;194(1):284-93. doi: 10.1006/viro.1993.1259.
Two kinds of unrelated African swine fever virus proteins of 220 kDa have been identified by means of two-dimensional gel electrophoresis and immunoprecipitation analysis. One species, named pp220 and identified as the precursor of the major structural protein p150, was found to be a moderately acidic protein (pl near 7) expressed after the replication of the viral DNA. The second species, a cluster of 220-kDa proteins with slightly different isoelectric points (pl ranging from 5 to 6), was found to be a homooligomeric complex formed by an early 32-kDa protein. This component was identified as the viral phosphoprotein p32, the most immunogenic early protein of African swine fever virus. A detailed characterization of its oligomeric structure is reported.
通过二维凝胶电泳和免疫沉淀分析，已鉴定出两种不相关的220 kDa非洲猪瘟病毒蛋白。其中一种名为pp220，被鉴定为主要结构蛋白p150的前体，发现它是一种中等酸性蛋白（pI接近7），在病毒DNA复制后表达。第二种是一组等电点略有不同（pI范围为5至6）的220 kDa蛋白，发现它是由一种早期32 kDa蛋白形成的同源寡聚复合物。该成分被鉴定为病毒磷蛋白p32，即非洲猪瘟病毒最具免疫原性的早期蛋白。本文报道了其寡聚结构的详细特征。
