Mutational analysis of the structure-function relationship of the leukemogenic membrane glycoprotein (GP55) of Friend spleen focus-forming virus (F-SFFV)
Amanuma, H.; Yugawa, T.; Watanabe, N.; Ikawa, Y.
Leukemia 11(Suppl 3): 160-161
1997
ISSN/ISBN: 0887-6924 PMID: 9209329 Document Number: 469582
Friend spleen focus-forming virus (F-SFFV) causes acute erythroleukemia in adult mice. F-SFFV encodes an envelope protein-like membrane glycoprotein called gp55 in its defective env gene. Gp55 is responsible for the early stage of leukemogenesis by F-SFFV by specifically binding to and activating the murine erythropoietin receptor (EPO-R). Gp55 has a polytropic env sequence in its N-terminal portion. This portion probably contains the binding site for the EPO-R. In order to obtain a clue for the structure of the binding site to the EPO-R, we isolated and analyzed many spontaneous revertant F-SFFVs which derived from the non-leukemogenic mutant F-SFFV having an ecotropic env sequence instead of the polytropic env sequence in its gp55 gene.