Chimeric envelope glycoproteins constructed between amphotropic and xenotropic murine leukemia retroviruses.
A set of chimeric envelope proteins between amphotropic and xenotropic murine leukemia retroviruses (MuLV), two closely related members in the MuLV family, were constructed. The purpose was to examine the regions that could be successfully exchanged between these two similar viral envelope proteins. The data indicate that fully active chimeras can be built when the junction is either at the EcoRI site (amino acid 169) 42 amino acids N-terminal to the polyproline hinge of gp70 (named CH4) or at the ScaI site (aa 593) in the membrane spanning portion of p15E (CH1). However, a chimera at the AflII site (aa 125, CH5) and two in the C-terminal end of gp70 (aa 418, CH2; aa 326, CH3) were inactive. These results, taken together with other data from our laboratory and others, suggest that the entire gp70/p15E structure is sensitive to alterations and that even envelope proteins that are very similar have only a limited ability to exchange sequences.
D016475:3T3 Cells; D000818:Animals; D016477:Artifacts; D001483:Base Sequence; D015153:Blotting, Western; D002460:Cell Line; D004279:DNA, Viral; D009052:Leukemia Virus, Murine / Q000235:genetics*; D051379:Mice; D008969:Molecular Sequence Data; D011993:Recombinant Fusion Proteins / Q000235:genetics / Q000378:metabolism; D014759:Viral Envelope Proteins / Q000235:genetics* / Q000378:metabolism
D004279:DNA, Viral; D011993:Recombinant Fusion Proteins; D014759:Viral Envelope Proteins