Isolation of a Transformation-defective Mutant of the McDonough Strain of Feline Sarcoma Virus Exhibiting Tyrosine Kinase Activity in Vitro but Not in Vivo

Overview

Journal J Virol

Publisher American Society for Microbiology

Date 1988 Jun 1

PMID 2835515

Citations 3

Authors

T Tamura

D Hennig

M Grell

H Niemann

B Boschek

Affiliations

Soon will be listed here.

Abstract

NRK cells transformed by the McDonough strain of feline sarcoma virus (SM-FeSV) were mutagenized by the use of 5'-azacytidine. Four cell lines expressing different transformation-defective phenotypes were isolated. Superinfection of these cell lines with simian sarcoma-associated virus (SSAV) led in three instances to the recovery of transforming virus particles carrying an intact fms gene. A nonconditional transformation-defective virus, designated td26-SM-FeSV (SSAV), was isolated from one of the cell lines. NRK cells infected with this mutant contained actin cables and fibronectin networks and exhibited normal cell morphology. Such cells formed only small colonies in soft agar and exhibited a mitogenic activity similar to that of noninfected cells. Cells infected with td26-SM-FeSV (SSAV) synthesized a gag-fms fusion glycoprotein (gp180gag-fms). This polypeptide was processed in the normal manner into the intracellular gp120v-fms and a transformation-defective gp140td-v-fms which was expressed at the surface of infected cells. This species had an increased electrophoretic mobility on polyacrylamide gels compared with the molecule from wild-type virus.gp140td-v-fms had endo-beta-N-acetylglucosaminidase H-resistant carbohydrate side chains. No tyrosine kinase activity was detectable in vivo in td26-SM-FeSV (SSAV)-infected cells even when the cells were treated with sodium orthovanadate. In vitro, fms molecules from td26-SM-FeSV (SSAV)-infected cells exhibited tyrosine kinase activity as determined by autophosphorylation and phosphorylation of exogenous (poly)Glu-Tyr. At low ATP concentrations (less than 5 microM) this in vitro tyrosine kinase activity was significantly reduced compared with that of the wild-type counterpart.

Citing Articles

Tyrosine 807 of the v-Fms oncogene product controls cell morphology and association with p120RasGAP.

Trouliaris S, Smola U, Chang J, Parsons S, Niemann H, Tamura T J Virol. 1995; 69(10):6010-20.

PMID: 7666506 PMC: 189497. DOI: 10.1128/JVI.69.10.6010-6020.1995.

Influence of tyrosine residues Y705 and Y807 on the transforming potency of the v-fms oncogene product of feline sarcoma virus.

Trouliaris S, Hadwiger-Fangmeier A, Heimann M, Tamura T Arch Virol. 1995; 140(1):179-86.

PMID: 7646343 DOI: 10.1007/BF01309733.

Reassessment of the v-fms sequence: threonine phosphorylation of the COOH-terminal domain.

Smola U, Hennig D, Hadwiger-Fangmeier A, Schutz B, Pfaff E, Niemann H J Virol. 1991; 65(11):6181-7.

PMID: 1833563 PMC: 250307. DOI: 10.1128/JVI.65.11.6181-6187.1991.

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