Disease relevance of gag

• Foamy viruses (FVs) generate their Pol protein precursor molecule independently of the Gag protein from a spliced mRNA [1].
• Furthermore, virions derived from a vector lacking this sequence were found to be deficient in the cleavage of the Gag protein by the Pol precursor protease [2].
• This motif was also found to be able to direct a heterologous protein, the Gag protein of human immunodeficiency virus, into the nucleus [3].
• The biological significance of the data was confirmed by mutational analysis of the cleavage sites in a recombinant Gag protein and in the context of the infectious HSRV DNA provirus [4].
• Taken together, our results suggest that the Gag protein of HFV may be more analogous to the core protein of the hepatitis B virus family than to conventional retroviral Gag protein [5].

High impact information on gag

• FV Gag protein was found to be phosphorylated at serine residues [6].
• This finding thus provides a direct evidence that although the sequences in GR box II can serve as a nuclear transport signal, they are not required for HFV replication and it is unlikely that nuclear localization of Gag protein plays any critical role during viral infection [5].
• By using HFV Gag protein substrates, the purified recombinant HFV PR was enzymatically active whereas the corresponding active site PR mutant Asp/Ala was inactive [7].

References