Identification of conformational and cold-sensitive mutations in the MuLV envelope protein.
The structure and function of the C-terminal domain of the murine leukemia virus Surface protein (MuLV SU) is not well defined. Passage of chimeric ecotropic-amphotropic MuLV viruses with junctions within the SU C-terminus results in the selection of specific point mutations which improve virus viability and Env function. Point mutations were characterized that alter the conformation of the SU/TM heterodimers on the viral particles. Mutation of position E311 within the Moloney MuLV SU protein alters the conformation of the TM protein and its recognition by antibody 42-114 in immunoprecipitation reactions. Mutation of either G541R in the amphotropic 4070A TM, V421M in the 4070A SU, or deletion of S39 and P40 at the N-terminus of the M-MuLV SU results in an irreversible cold-sensitive phenotype at 4 degrees C. This loss of viral titer can be restored by incorporating V421M plus G541R or del S39 P40 plus G541R in cis within the SU/TM.
O'Reilly
Lucille
L
Department of Biochemistry, University of Medicine and Dentistry of New Jersey-Robert Wood Johnson Medical School, 675 Hoes Lane, Piscataway, NJ 08854, USA.
Roth
Monica J
MJ
D000818:Animals; D002460:Cell Line; D003080:Cold Temperature; D004274:DNA, Recombinant; D004285:Dogs; D009052:Leukemia Virus, Murine / Q000737:chemistry* / Q000235:genetics*; D008958:Models, Molecular; D010641:Phenotype; D017354:Point Mutation / Q000235:genetics; D011487:Protein Conformation; D014759:Viral Envelope Proteins / Q000737:chemistry* / Q000235:genetics* / Q000378:metabolism
D004274:DNA, Recombinant; D014759:Viral Envelope Proteins