Rescue of internal scaffold-deleted Mason-Pfizer monkey virus particle production by plasma membrane targeting.
The Mason-Pfizer monkey virus (M-PMV) Gag protein follows a morphogenesis pathway in which immature capsids are preassembled within the cytoplasm before interaction with and budding through the plasma membrane. Intracytoplasmic assembly is facilitated by sequences within the p12 domain of Gag that we have termed the Internal Scaffold Domain (ISD). If M-PMV utilizes an ISD then what provides the equivalent function for most other retroviruses that assemble at the plasma membrane? To investigate the possibility that the membrane itself fulfills this role, we have combined functional deletion of the ISD with a mutation that disrupts intracellular targeting or with a plasma membrane targeting signal. By either modification, targeting of ISD-deleted Gag to the plasma membrane restores particle production. These results provide support for a model in which the plasma membrane and the D-type ISD provide an interchangeable scaffold-like function in retrovirus assembly.
Sakalian
Michael
M
Department of Microbiology and Immunology, The University of Oklahoma Health Sciences Center, 940 Stanton L. Young Boulevard, Oklahoma City, 73104, USA. mike-sakalian@ouhsc.edu
Rapp
Nathan D
ND
D000818:Animals; D002213:Capsid; D002462:Cell Membrane / Q000378:metabolism*; D015683:Gene Products, gag / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D006367:HeLa Cells; D006801:Humans; D016093:Mason-Pfizer monkey virus / Q000235:genetics / Q000378:metabolism*; D017384:Sequence Deletion; D014771:Virion / Q000378:metabolism*; D019065:Virus Assembly
D015683:Gene Products, gag