Electrochemical modification of vesicular stomatitis virus glycoprotein by host cell transformation.
Electrochemical properties of the glycoprotein of vesicular stomatitis virus (VSV) grown in Rous sarcoma virus (RSV)-transformed cells was compared with that of its counterpart grown in nontransformed cells. In DEAE-Sephadex column chromatography, the glycoproteins of VSV derived from transformed cells appeared more heterogeneous and had a tendency to elute with higher concentrations of NaCl than those from nontransformed cells. In isoelectric focussing, the glycoproteins of VSVs derived from transformed and nontransformed cells appeared as multiple components differing in the isoelectric point, and the glycoproteins from virus from transformed cells had isoelectric points that were more acidic than their counterparts from nontransformed cells. These results show that the glycoprotein of VSV consists of populations of molecules differing in charge and their isoelectric points were shifted to the acidic side by host cell transformation.
D000818:Animals; D001358:Avian Sarcoma Viruses / Q000502:physiology; D002472:Cell Transformation, Viral; D002478:Cells, Cultured; D002642:Chick Embryo; D002852:Chromatography, Ion Exchange; D006023:Glycoproteins / Q000032:analysis*; D007526:Isoelectric Point; D014721:Vesicular stomatitis Indiana virus / Q000032:analysis* / Q000254:growth & development; D014764:Viral Proteins / Q000032:analysis*
D006023:Glycoproteins; D014764:Viral Proteins