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Gene Review

gag  -  gag

Simian foamy virus

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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].


  1. RNA and protein requirements for incorporation of the Pol protein into foamy virus particles. Peters, K., Wiktorowicz, T., Heinkelein, M., Rethwilm, A. J. Virol. (2005) [Pubmed]
  2. Characterization of a cis-acting sequence in the Pol region required to transfer human foamy virus vectors. Heinkelein, M., Schmidt, M., Fischer, N., Moebes, A., Lindemann, D., Enssle, J., Rethwilm, A. J. Virol. (1998) [Pubmed]
  3. Nuclear localization of foamy virus Gag precursor protein. Schliephake, A.W., Rethwilm, A. J. Virol. (1994) [Pubmed]
  4. Molecular characterization of proteolytic processing of the Gag proteins of human spumavirus. Pfrepper, K.I., Löchelt, M., Rackwitz, H.R., Schnölzer, M., Heid, H., Flügel, R.M. J. Virol. (1999) [Pubmed]
  5. The carboxyl terminus of the human foamy virus Gag protein contains separable nucleic acid binding and nuclear transport domains. Yu, S.F., Edelmann, K., Strong, R.K., Moebes, A., Rethwilm, A., Linial, M.L. J. Virol. (1996) [Pubmed]
  6. Carboxy-terminal cleavage of the human foamy virus Gag precursor molecule is an essential step in the viral life cycle. Enssle, J., Fischer, N., Moebes, A., Mauer, B., Smola, U., Rethwilm, A. J. Virol. (1997) [Pubmed]
  7. Expression and molecular characterization of an enzymatically active recombinant human spumaretrovirus protease. Pfrepper, K.I., Löchelt, M., Schnölzer, M., Flügel, R.M. Biochem. Biophys. Res. Commun. (1997) [Pubmed]
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