title: Human foamy virus capsid formation requires an interaction domain in the N terminus of Gag.
abstract: Retroviral Gag expression is sufficient for capsid assembly, which occurs through interaction between distinct Gag domains. Human foamy virus (HFV) capsids assemble within the cytoplasm, although their budding, which mainly occurs in the endoplasmic reticulum, requires the presence of homologous Env. Yet little is known about the molecular basis of HFV Gag precursor assembly. Using fusions between HFV Gag and a nuclear reporter protein, we have identified a strong interaction domain in the N terminus of HFV Gag which is predicted to contain a conserved coiled-coil motif. Deletion within this region in an HFV provirus abolishes viral production through inhibition of capsid assembly.
authors: CNRS UPR9051, Hôpital Saint-Louis, Université Paris 7, 75475 Paris Cedex 10, France.
authors: J
authors: J
authors: Tobaly-Tapiero
authors: P
authors: P
authors: Bittoun
authors: M L
authors: ML
authors: Giron
authors: M
authors: M
authors: Neves
authors: M
authors: M
authors: Koken
authors: A
authors: A
authors: Saïb
authors: H
authors: H
authors: de Thé
mesh_terms: D016475:3T3 Cells; D000595:Amino Acid Sequence; D000818:Animals; D001665:Binding Sites; D019556:COS Cells; D002213:Capsid / Q000502:physiology*; D002460:Cell Line; D002522:Chlorocebus aethiops; D002874:Chromosome Mapping; D006224:Cricetinae; D015683:Gene Products, gag / Q000235:genetics / Q000378:metabolism*; D006801:Humans; D051379:Mice; D008969:Molecular Sequence Data; D016092:Spumavirus / Q000378:metabolism / Q000502:physiology*; D019065:Virus Assembly / Q000502:physiology*
chemical_list: D015683:Gene Products, gag