The Fv-2 Gene Controls Induction of Erythroid Burst Formation by Friend Virus Infection in vitro: Studies of Growth Regulators and Viral Replication

Bondurant, Maurice C.; Koury, Mark J.; Krantz, Sanford B.

doi:10.1099/0022-1317-66-1-83

Cited by 11 publications

(3 citation statements)

References 25 publications

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“…Following in vitro infection with the polycythemia-inducing strain of Friend virus (FVP), these cells were plated in a minimal methylcellulose media supplemented with interleukin-3 (IL-3) and then assessed for their ability to form Epo-independent erythroid colonies (CFU-E) and bursts (BFU-E). As shown previously, bone marrow cells from Fv2 ss BALB/c mice, but not Fv2 rr C57BL/6 mice, incubated with Friend virus are able to form Epo-independent CFU-E and BFU-E (Figure 1a,b; (Bondurant et al, 1985;Clarke et al, 1975)). Bone marrow cells from Fv2 rr C57BL/6 mice were then incubated with viral particles expressing vector alone or a myc-tagged Sf-Stk.…”

Section: Sf-stk Expression Confers Friend Virus Sensitivity In Vitromentioning

confidence: 82%

Sf-Stk kinase activity and the Grb2 binding site are required for Epo-independent growth of primary erythroblasts infected with Friend virus

et al. 2002

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Section: Sf-stk Expression Confers Friend Virus Sensitivity In Vitromentioning

confidence: 82%

Sf-Stk kinase activity and the Grb2 binding site are required for Epo-independent growth of primary erythroblasts infected with Friend virus

et al. 2002

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“…Although sf-Stk appears to be essential for the development of Epo-independent erythroid bursts after in vitro infection with SFFV (3,14) and for the development of SFFV-induced erythroleukemia (22), it was surprising to find that it is not required for the induction of Epo independence by SFFV gp55 in BaF3-EpoR cells. This suggests that BaF3-EpoR cells, which are pro-B cells (31), express another tyrosine kinase that can be activated by SFFV gp55.…”

Section: Discussionmentioning

confidence: 99%

“…Most of these host genes interfere with viral entry or integration, or they control immune responses against the virus-infected cells (for a review, see reference 7). However, the Fv-2 gene (22), which is located on mouse chromosome 9, acts at the level of the erythroid target cell for the virus (2,3,9,13,39). Mice carrying at least one copy of the Fv-2 s allele are susceptible to SFFV-induced erythroleukemia, and their erythroid cells will form Epo-independent erythroid bursts when infected in vitro with SFFV.…”

mentioning

confidence: 99%

The Envelope Glycoprotein of Friend Spleen Focus-Forming Virus Covalently Interacts with and Constitutively Activates a Truncated Form of the Receptor Tyrosine Kinase Stk

Nishigaki

Thompson

Hanson

et al. 2001

J Virol

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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.The Friend spleen focus-forming virus (SFFV) causes an acute erythroleukemia in susceptible strains of mice (for a review, see reference 37). SFFV encodes a unique envelope glycoprotein, gp55, that associates specifically with the erythropoietin receptor (EpoR) at the cell surface (4, 10, 21, 45), allowing erythroid cells to proliferate in the absence of erythropoietin (Epo), the normal regulator of erythropoiesis. Epo stimulation of the EpoR activates a number of signal transduction pathways, including the Jak-Stat, the Ras/Raf-1/mitogenactivated protein kinase (MAPK), and the phosphatidylinositol 3-kinase (PI3-kinase) pathways (for a review, see reference 46). Using the Epo-dependent erythroleukemia cell line HCD-57, we have previously demonstrated that infection with SFFV, which abrogates the Epo dependence of these cells (36), constitutively activates Stat DNA-binding activity (30); Ras (27); Raf-1, MEK, and MAPK (26); PI 3-kinase and Akt kinase (29); and protein kinase C (27).Although interaction of the SFFV envelope glycoprotein with the EpoR complex is essential for inducing the biological effects of the virus, other f...

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Retroviruses and Their Role in Cancer

Fan

1994

The Retroviridae

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The Fv-2 Gene Controls Induction of Erythroid Burst Formation by Friend Virus Infection in vitro: Studies of Growth Regulators and Viral Replication

Cited by 11 publications

References 25 publications

Sf-Stk kinase activity and the Grb2 binding site are required for Epo-independent growth of primary erythroblasts infected with Friend virus

Sf-Stk kinase activity and the Grb2 binding site are required for Epo-independent growth of primary erythroblasts infected with Friend virus

The Envelope Glycoprotein of Friend Spleen Focus-Forming Virus Covalently Interacts with and Constitutively Activates a Truncated Form of the Receptor Tyrosine Kinase Stk

Retroviruses and Their Role in Cancer

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