Neipel F, Ellinger K, Fleckenstein B
Institut für klinische und molekulare Virologie, Universität Erlangen-Nürnberg, Germany.
J Virol. 1992 Jun;66(6):3918-24. doi: 10.1128/JVI.66.6.3918-3924.1992.
A human herpesvirus 6 (HHV-6) structural protein of 100 kDa (p100) is the polypeptide most frequently and intensively reactive in immunoblotting analyses with human sera on HHV-6-infected cells or partially purified virions. The gene for p100 was identified by screening a bacteriophage lambda library with monospecific rabbit antisera. The gene codes for a polypeptide of 870 amino acids with a calculated molecular size of 97 kDa. Its amino-terminal third is weakly homologous to the immunogenic basic matrix phosphoprotein pp150 of human cytomegalovirus. Five fragments representing more than 93% of HHV-6 p100 were prokaryotically expressed. The antigenic epitopes of p100 were preliminary mapped by immunoblotting with human sera. They are located within the carboxy-terminal part which is neither homologous nor cross-reactive to pp150 of human cytomegalovirus. Availability of the gene for the immunodominant structural protein should provide tools for studies of pathogenesis by HHV-6.
人疱疹病毒6型(HHV-6)的一种100 kDa结构蛋白(p100)是在用人类血清对HHV-6感染细胞或部分纯化病毒体进行免疫印迹分析时,反应最频繁且强烈的多肽。通过用单特异性兔抗血清筛选λ噬菌体文库鉴定了p100的基因。该基因编码一种870个氨基酸的多肽,计算分子量为97 kDa。其氨基末端的三分之一与人巨细胞病毒的免疫原性碱性基质磷蛋白pp150有弱同源性。代表HHV-6 p100超过93%的五个片段在原核中表达。通过用人血清进行免疫印迹初步定位了p100的抗原表位。它们位于羧基末端部分,与人巨细胞病毒的pp150既不同源也无交叉反应。这种免疫显性结构蛋白基因的可用性应为研究HHV-6的发病机制提供工具。