Abstract:
:The Spumaretrovirinae, or foamy viruses (FVs) are complex retroviruses that infect many species of monkey and ape. Despite little sequence homology, FV and orthoretroviral Gag proteins perform equivalent functions, including genome packaging, virion assembly, trafficking and membrane targeting. However, there is a paucity of structural information for FVs and it is unclear how disparate FV and orthoretroviral Gag molecules share the same function. To probe the functional overlap of FV and orthoretroviral Gag we have determined the structure of a central region of Gag from the Prototype FV (PFV). The structure comprises two all α-helical domains NtDCEN and CtDCEN that although they have no sequence similarity, we show they share the same core fold as the N- (NtDCA) and C-terminal domains (CtDCA) of archetypal orthoretroviral capsid protein (CA). Moreover, structural comparisons with orthoretroviral CA align PFV NtDCEN and CtDCEN with NtDCA and CtDCA respectively. Further in vitro and functional virological assays reveal that residues making inter-domain NtDCEN-CtDCEN interactions are required for PFV capsid assembly and that intact capsid is required for PFV reverse transcription. These data provide the first information that relates the Gag proteins of Spuma and Orthoretrovirinae and suggests a common ancestor for both lineages containing an ancient CA fold.
journal_name
PLoS Pathogjournal_title
PLoS pathogensauthors
Ball NJ,Nicastro G,Dutta M,Pollard DJ,Goldstone DC,Sanz-Ramos M,Ramos A,Müllers E,Stirnnagel K,Stanke N,Lindemann D,Stoye JP,Taylor WR,Rosenthal PB,Taylor IAdoi
10.1371/journal.ppat.1005981subject
Has Abstractpub_date
2016-11-09 00:00:00pages
e1005981issue
11eissn
1553-7366issn
1553-7374pii
PPATHOGENS-D-16-01565journal_volume
12pub_type
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