title: Definition of an amino-terminal domain of the human T-cell leukemia virus type 1 envelope surface unit that extends the fusogenic range of an ecotropic murine leukemia virus.
abstract: Murine leukemia viruses (MuLV) and human T-cell leukemia viruses (HTLV) are phylogenetically highly divergent retroviruses with distinct envelope fusion properties. The MuLV envelope glycoprotein surface unit (SU) comprises a receptor-binding domain followed by a proline-rich region which modulates envelope conformational changes and fusogenicity. In contrast, the receptor-binding domain and SU organization of HTLV are undefined. Here, we describe an HTLV/MuLV envelope chimera in which the receptor-binding domain and proline-rich region of the ecotropic MuLV were replaced with the potentially corresponding domains of the HTLV-1 SU. This chimeric HTLV/MuLV envelope was processed, specifically interfered with HTLV-1 envelope-mediated fusion, and similar to MuLV envelopes, required cleavage of its cytoplasmic tail to exert significant fusogenic properties. Furthermore, the HTLV domain defined here broadened ecotropic MuLV envelope-induced fusion to human and simian cell lines.
authors.affiliation: Institut de Génétique Moléculaire de Montpellier, IFR24, CNRS-UMR5535, Paris, France.
authors.forename: F J
authors.initials: FJ
authors.lastname: Kim
authors.forename: I
authors.initials: I
authors.lastname: Seiliez
authors.forename: C
authors.initials: C
authors.lastname: Denesvre
authors.forename: D
authors.initials: D
authors.lastname: Lavillette
authors.forename: F L
authors.initials: FL
authors.lastname: Cosset
authors.forename: M
authors.initials: M
authors.lastname: Sitbon
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D001665:Binding Sites; D002460:Cell Line; D017124:Conserved Sequence; D005622:Friend murine leukemia virus / Q000737:chemistry* / Q000235:genetics; D006023:Glycoproteins / Q000096:biosynthesis / Q000737:chemistry* / Q000235:genetics; D015368:Human T-lymphotropic virus 1 / Q000737:chemistry*; D006801:Humans; D008561:Membrane Fusion; D051379:Mice; D008969:Molecular Sequence Data; D011323:Primates; D011392:Proline; D011499:Protein Processing, Post-Translational; D011993:Recombinant Fusion Proteins / Q000096:biosynthesis; D017386:Sequence Homology, Amino Acid; D014759:Viral Envelope Proteins / Q000096:biosynthesis / Q000737:chemistry* / Q000235:genetics; D014760:Viral Fusion Proteins / Q000096:biosynthesis / Q000737:chemistry* / Q000235:genetics
chemical_list: D006023:Glycoproteins; D011993:Recombinant Fusion Proteins; D014759:Viral Envelope Proteins; D014760:Viral Fusion Proteins; D011392:Proline