Abstract
Background Foamy viruses (FVs) are distinct retroviruses with several features of their molecular biology and replication strategy clearly different from those of Orthoretroviruses like HIV, MLV and HTLV. One distinguishing feature of FVs is the absolute dependence of the cognate Env protein for Gag particle budding. Recent data showed that Gag has the capacity to bud from the cell, provided that a heterologous myristoylation signal is N-terminally appended. When this interaction is engineered to be reversible, even infectious particles are released. While the interaction surface of the FV-specific Env leader protein Elp required to specifically interact with Gag has been characterized to some degree, we set out to characterize the corresponding domain of Gag by separating the budding-relevant functions from those required for FV cytosolic Gag assembly.
Highlights
Foamy viruses (FVs) are distinct retroviruses with several features of their molecular biology and replication strategy clearly different from those of Orthoretroviruses like HIV, MLV and HTLV
N-terminal foamy virus Gag domains and individual residues are critical for capsid assembly and interaction with the unique Env leader protein Elp for Env-dependent budding
While the interaction surface of the FV-specific Env leader protein Elp required to interact with Gag has been characterized to some degree, we set out to characterize the corresponding domain of Gag by separating the budding-relevant functions from those required for FV cytosolic Gag assembly
Summary
Foamy viruses (FVs) are distinct retroviruses with several features of their molecular biology and replication strategy clearly different from those of Orthoretroviruses like HIV, MLV and HTLV. One distinguishing feature of FVs is the absolute dependence of the cognate Env protein for Gag particle budding. Recent data showed that Gag has the capacity to bud from the cell, provided that a heterologous myristoylation signal is N-terminally appended. When this interaction is engineered to be reversible, even infectious particles are released. While the interaction surface of the FV-specific Env leader protein Elp required to interact with Gag has been characterized to some degree, we set out to characterize the corresponding domain of Gag by separating the budding-relevant functions from those required for FV cytosolic Gag assembly
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