Structure of a Spumaretrovirus Gag Central Domain Reveals an Ancient Retroviral Capsid

• DOI: 10.1371/journal.ppat.1005981
• Publication Date: 2016-11-09T18:43:48Z
• Authors: Neil J. Ball; Giuseppe Nicastro; Moumita Dutta; Dominic J. Pollard; David C. Goldstone; Marta Sanz-Ramos; Andres Ramos; Erik Müllers; Kristin Stirnnagel; Nicole Stanke; Dirk Lindemann; Jonathan P. Stoye; William R. Taylor; Peter B. Rosenthal; Ian A. Taylor
• Keywords: Group-specific antigen

The Spumaretrovirinae, or foamy viruses (FVs) are complex retroviruses that infect many species of monkey and ape. Despite little sequence homology, FV orthoretroviral Gag proteins perform equivalent functions, including genome packaging, virion assembly, trafficking membrane targeting. However, there is a paucity structural information for FVs it unclear how disparate molecules share the same function. To probe functional overlap we have determined structure central region from Prototype (PFV). comprises two all α-helical domains NtDCEN CtDCEN although they no similarity, show core fold as N- (NtDCA) C-terminal (CtDCA) archetypal capsid protein (CA). Moreover, comparisons with CA align PFV NtDCA CtDCA respectively. Further in vitro virological assays reveal residues making inter-domain NtDCEN-CtDCEN interactions required assembly intact reverse transcription. These data provide first relates Spuma Orthoretrovirinae suggests common ancestor both lineages containing an ancient fold.