Nishigaki K, Thompson D, Hanson C, Yugawa T, Ruscetti S
Basic Research Laboratory, National Cancer Institute, Frederick, Maryland 21702-1201, USA.
J Virol. 2001 Sep;75(17):7893-903. doi: 10.1128/jvi.75.17.7893-7903.2001.
The Friend spleen focus-forming virus (SFFV) encodes a unique envelope glycoprotein, gp55, which allows erythroid cells to proliferate and differentiate in the absence of erythropoietin (Epo). SFFV gp55 has been shown to interact with the Epo receptor complex, causing constitutive activation of various signal-transducing molecules. When injected into adult mice, SFFV induces a rapid erythroleukemia, with susceptibility being determined by the host gene Fv-2, which was recently shown to be identical to the gene encoding the receptor tyrosine kinase Stk/Ron. Susceptible, but not resistant, mice encode not only full-length Stk but also a truncated form of the kinase, sf-Stk, which may mediate the biological effects of SFFV infection. To determine whether expression of SFFV gp55 leads to the activation of sf-Stk, we expressed sf-Stk, with or without SFFV gp55, in hematopoietic cells expressing the Epo receptor. Our data indicate that sf-Stk interacts with SFFV gp55 as well as gp55(P), the biologically active form of the viral glycoprotein, forming disulfide-linked complexes. This covalent interaction, as well as noncovalent interactions with SFFV gp55, results in constitutive tyrosine phosphorylation of sf-Stk and its association with multiple tyrosine-phosphorylated signal-transducing molecules. In contrast, neither Epo stimulation in the absence of SFFV gp55 expression nor expression of a mutant of SFFV that cannot interact with sf-Stk was able to induce tyrosine phosphorylation of sf-Stk or its association with any signal-transducing molecules. Covalent interaction of sf-Stk with SFFV gp55 and constitutive tyrosine phosphorylation of sf-Stk can also be detected in an erythroleukemia cell line derived from an SFFV-infected mouse. Our results suggest that SFFV gp55 may mediate its biological effects in vivo by interacting with and activating a truncated form of the receptor tyrosine kinase Stk.
Friend脾集落形成病毒(SFFV)编码一种独特的包膜糖蛋白gp55,它能使红系细胞在无促红细胞生成素(Epo)的情况下增殖和分化。已证明SFFV gp55可与Epo受体复合物相互作用,导致各种信号转导分子的组成性激活。将SFFV注入成年小鼠后,会诱发快速的红白血病,其易感性由宿主基因Fv - 2决定,最近发现该基因与编码受体酪氨酸激酶Stk/Ron的基因相同。易感但非抗性的小鼠不仅编码全长Stk,还编码激酶的截短形式sf - Stk,它可能介导SFFV感染的生物学效应。为了确定SFFV gp55的表达是否导致sf - Stk的激活,我们在表达Epo受体的造血细胞中表达了有或无SFFV gp55的sf - Stk。我们的数据表明,sf - Stk与SFFV gp55以及病毒糖蛋白的生物活性形式gp55(P)相互作用,形成二硫键连接的复合物。这种共价相互作用以及与SFFV gp55的非共价相互作用,导致sf - Stk的组成性酪氨酸磷酸化及其与多种酪氨酸磷酸化信号转导分子的结合。相比之下,在无SFFV gp55表达时的Epo刺激或不能与sf - Stk相互作用的SFFV突变体的表达,均不能诱导sf - Stk的酪氨酸磷酸化或其与任何信号转导分子的结合。在源自SFFV感染小鼠的红白血病细胞系中,也能检测到sf - Stk与SFFV gp55的共价相互作用以及sf - Stk的组成性酪氨酸磷酸化。我们的结果表明,SFFV gp55可能通过与受体酪氨酸激酶Stk的截短形式相互作用并激活它,在体内介导其生物学效应。