Lauring A S, Anderson M M, Overbaugh J
Program in Molecular and Cellular Biology, University of Washington, Seattle, USA.
J Virol. 2001 Oct;75(19):8888-98. doi: 10.1128/JVI.75.19.8888-8898.2001.
Cytopathic, T-cell-tropic feline leukemia viruses (FeLV-T) evolve from FeLV-A in infected animals and demonstrate host cell specificities that are distinct from those of their parent viruses. We recently identified two cellular proteins, FeLIX and Pit1, required for productive infection by these immunodeficiency-inducing FeLV-T variants (M. M. Anderson, A. S. Lauring, C. C. Burns, and J. Overbaugh, Science 287:1828-1830, 2000). FeLV-T is the first example of a naturally occurring type C retrovirus that requires two proteins to gain entry into target cells. FeLIX is an endogenous protein that is highly related to the N-terminal portion of the FeLV envelope protein, which includes the receptor-binding domain. Pit1 is a multiple-transmembrane phosphate transport protein that also functions as a receptor for FeLV-B. The FeLV-B envelope gene is derived by recombination with endogenous FeLV-like sequences, and its product can functionally substitute for FeLIX in facilitating entry through the Pit1 receptor. In the present study, we tested other retrovirus envelope surface units (SUs) with their cognate receptors to determine whether they also could mediate infection by FeLV-T. Cells were engineered to coexpress the transmembrane form of the envelope proteins and their cognate receptors, or SU protein was added as a soluble protein to cells expressing the receptor. Of the FeLV, murine leukemia virus, and gibbon ape leukemia virus envelopes tested, we found that only those with receptor-binding domains derived from endogenous FeLV could render cells permissive for FeLV-T. We also found that there is a strong preference for Pit1 as the transmembrane receptor. Specifically, FeLV-B SUs could efficiently mediate infection of cells expressing the Pit1 receptor but could only inefficiently mediate infection of cells expressing the Pit2 receptor, even though these SUs are able to bind to Pit2. Expression analysis of feline Pit1 and FeLIX suggests that FeLIX is likely the primary determinant of FeLV-T tropism. These results are discussed in terms of current models for retrovirus entry and the interrelationship among FeLV variants that evolve in vivo.
细胞病变性、嗜T细胞的猫白血病病毒(FeLV-T)在受感染动物体内由FeLV-A进化而来,其宿主细胞特异性与其亲本病毒不同。我们最近鉴定出两种细胞蛋白,FeLIX和Pit1,它们是这些诱导免疫缺陷的FeLV-T变体进行有效感染所必需的(M.M.安德森、A.S.劳林、C.C.伯恩斯和J.奥弗鲍尔,《科学》287:1828 - 1830,2000)。FeLV-T是天然存在的C型逆转录病毒中首个需要两种蛋白才能进入靶细胞的例子。FeLIX是一种内源性蛋白,与FeLV包膜蛋白的N端部分高度相关,该部分包括受体结合结构域。Pit1是一种多跨膜磷酸盐转运蛋白,也作为FeLV-B的受体发挥作用。FeLV-B包膜基因通过与内源性FeLV样序列重组产生,其产物在促进通过Pit1受体进入细胞的过程中可在功能上替代FeLIX。在本研究中,我们用其他逆转录病毒包膜表面单位(SUs)及其同源受体进行测试,以确定它们是否也能介导FeLV-T的感染。对细胞进行工程改造,使其共表达包膜蛋白的跨膜形式及其同源受体,或者将SU蛋白作为可溶性蛋白添加到表达受体的细胞中。在所测试的FeLV、鼠白血病病毒和长臂猿白血病病毒包膜中,我们发现只有那些受体结合结构域源自内源性FeLV的包膜才能使细胞对FeLV-T具有易感性。我们还发现强烈偏好Pit1作为跨膜受体。具体而言,FeLV-B SUs能够有效地介导表达Pit1受体的细胞的感染,但只能低效地介导表达Pit2受体的细胞的感染,尽管这些SUs能够与Pit2结合。猫Pit1和FeLIX的表达分析表明,FeLIX可能是FeLV-T嗜性的主要决定因素。根据当前的逆转录病毒进入模型以及体内进化的FeLV变体之间的相互关系对这些结果进行了讨论。