泡沫病毒能在宿主细胞内长期潜伏感染,且不伴随任何病理现象.为了阐明这一病毒潜伏感染机制,关键要研究病毒与其宿主之间的相互影响,尤其是宿主对病毒基因转录水平的影响.Bell是人泡沫病毒的反式激活因子,它能够激活该病毒LTR和IP两个转录启动子.该研究利用酵母双杂交技术筛选到Bell的相互作用蛋白α-Enolase,并用免疫共沉淀技术确定了这两个蛋白的结合涉及α-Enolase的243~372位氨基酸及Bell的223-275位氨基酸.细胞转染实验发现α-Enolase蛋白能够抑制Bell介导的反式激活作用.
Foamy viruses establish latency infections in the absence of accompanying pathology in a long-term. To understand the molecular mechanism, one of the biggest challenges lies in understanding the interactions of these viruses with their hosts. Although limited transcription is a prerequisite of FV latency, the factors that regulate this process are poorly understood. Bell, the key regulator of PFV, activates gene expression of PFV LTR and IP. Using the yeast two hybird screening, α-Enolase is identified as a novel potential cellular protein interacting with PFV Bell. α-Enolase specifically binds to Bell in coimmunoprecipitation assay and the binding between the two proteins require the portions of α-Enolase (243-372 aa) and Bell (223-275 aa). In addition,α-Enolase inhibits Bell-mediated activation of PFV LTR and IP.