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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

Kim, F. J.; Seiliez, I.; Denesvre, C.; Lavillette, D.; Cosset, F. L.; Sitbon, M.

J Biol Chem

2000-08-04 / vol 275 / pages 23417-20

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.

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Tags

Humans; Animals; Mice; Amino Acid Sequence; Molecular Sequence Data; Cell Line; Binding Sites; Protein Processing, Post-Translational; Sequence Homology, Amino Acid; Conserved Sequence; *Membrane Fusion; Friend murine leukemia virus/*chemistry/genetics; Glycoproteins/biosynthesis/*chemistry/genetics; Human T-lymphotropic virus 1/*chemistry; Primates; Proline; Recombinant Fusion Proteins/biosynthesis; Viral Envelope Proteins/biosynthesis/*chemistry/genetics; Viral Fusion Proteins/biosynthesis/*chemistry/genetics

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