Srinivas R V, Kilpatrick D R, Compans R W
Department of Microbiology, University of Alabama, Birmingham 35294.
J Virol. 1987 Dec;61(12):4007-11. doi: 10.1128/JVI.61.12.4007-4011.1987.
Friend murine spleen focus-forming virus (SFFV) encodes a glycoprotein designated gp52, which is responsible for the leukemogenic properties of the virus. gp52 lacks a cytoplasmic domain and is defective in its transport to the cell surface. We constructed a chimeric envelope gene which codes for a molecule with an external domain derived from the SFFV envelope gene and membrane-spanning and cytoplasmic domains derived from the Friend murine leukemia virus envelope gene. Like gp52, the chimeric protein was defective in its transport to the cell surface, indicating that the absence of a cytoplasmic tail is not responsible for the defective intracellular transport of SFFV gp52. However, unlike wild-type SFFV, the chimeric SFFV genome failed to induce erythroleukemia in adult mice. The results indicate that the altered membrane-spanning domain, lack of a detectable cytoplasmic tail in gp52, or both factors are prerequisites for the erythroleukemia-inducing properties of SFFV but are not responsible for the block in intracellular transport of the glycoprotein.
Friend小鼠脾集落形成病毒（SFFV）编码一种名为gp52的糖蛋白，该糖蛋白负责病毒的致白血病特性。gp52缺乏细胞质结构域，并且在向细胞表面的转运过程中存在缺陷。我们构建了一个嵌合包膜基因，该基因编码一种分子，其外部结构域源自SFFV包膜基因，跨膜结构域和细胞质结构域源自Friend小鼠白血病病毒包膜基因。与gp52一样，嵌合蛋白在向细胞表面的转运过程中存在缺陷，这表明细胞质尾巴的缺失并非SFFV gp52细胞内转运缺陷的原因。然而，与野生型SFFV不同，嵌合SFFV基因组未能在成年小鼠中诱导红白血病。结果表明，改变的跨膜结构域、gp52中缺乏可检测到的细胞质尾巴或这两个因素都是SFFV诱导红白血病特性的先决条件，但并非糖蛋白细胞内转运受阻的原因。
