PR domain of rous sarcoma virus Gag causes an assembly/budding defect in insect cells.
While baculovirus expression of Gag proteins from numerous retroviruses has led reliably to production of virus-like particles (VLPs), we observed that expression of Rous sarcoma virus Gag failed to produce VLPs. Transmission and scanning electron microscopy analysis revealed that the Gag protein reached the plasma membrane but was unable to correctly form particles. Addition of a myristylation signal had no effect on the budding defect, but deletion of the PR domain of Gag restored normal budding. The resulting VLPs were morphologically distinct from human immunodeficiency virus type 1 VLPs expressed in parallel.
Johnson
M C
MC
Department of Molecular Biology and Genetics, Cornell University, Ithaca, New York 14853, USA. mcj7@cornell.edu
Scobie
H M
HM
Vogt
V M
VM
D000818:Animals; D016282:Aspartic Acid Endopeptidases / Q000235:genetics / Q000502:physiology*; D001358:Avian Sarcoma Viruses / Q000502:physiology* / Q000648:ultrastructure; D002460:Cell Line; D003673:Defective Viruses / Q000502:physiology* / Q000648:ultrastructure; D015683:Gene Products, gag / Q000235:genetics / Q000502:physiology*; D006801:Humans; D018411:Spodoptera / Q000166:cytology; D019065:Virus Assembly / Q000502:physiology*
D015683:Gene Products, gag; D016282:Aspartic Acid Endopeptidases; C072891:Rous sarcoma virus protease