       Document 0790
 DOCN  M9590790
 TI    Influence of transmembrane domains on the fusogenic abilities of human
       and murine leukemia retrovirus envelopes.
 DT    9509
 AU    Denesvre C; Sonigo P; Corbin A; Ellerbrok H; Sitbon M; Institut Cochin
       de Genetique Moleculaire, CNRS UPR415,; Universite Paris V, France.
 SO    J Virol. 1995 Jul;69(7):4149-57. Unique Identifier : AIDSLINE
       MED/95287466
 AB    The envelopes of two highly divergent oncoviruses, human T-cell leukemia
       virus type 1 (HTLV-1) and Friend murine leukemia virus (F-MuLV), have
       distinct patterns of cellular receptor recognition, fusion, and
       syncytium formation. To analyze the influence of the transmembrane
       envelope subunit (TM) on fusogenic properties, we substituted either the
       entire TM or distinct domains from F-MuLV for the corresponding domains
       in the HTLV-1 envelope. Parental, chimeric, and truncated envelopes
       cloned into a eukaryotic expression vector were monitored for fusogenic
       potential in human, rat, and murine indicator cell lines by using a
       quantitative assay. This highly sensitive assay allowed us to assess the
       fusogenic properties and syncytium-forming abilities of the HTLV-1
       envelope in murine NIH 3T3 cells. All chimeric envelopes containing
       extracellular sequences of the F-MuLV TM were blocked in their
       maturation process. Although deletions of the HTLV-1 cytoplasmic domain,
       alone and in combination with the membrane-spanning domain, did not
       prevent envelope cell surface expression, they impaired and suppressed
       fusogenic properties, respectively. In contrast, envelopes carrying
       substitutions of membrane-spanning and cytoplasmic domains were highly
       fusogenic. Our results indicate that these two domains in F-MuLV and
       HTLV-1 constitute structural entities with similar fusogenic properties.
       However, in the absence of a cytoplasmic domain, the F-MuLV
       membrane-spanning domain appeared to confer weaker fusogenic properties
       than the HTLV-1 membrane-spanning domain.
 DE    Amino Acid Sequence  Animal  Base Sequence  Cell Fusion  Friend
       Virus/*PHYSIOLOGY  Genes, env  HTLV-I/*PHYSIOLOGY  Mice  Molecular
       Sequence Data  Support, Non-U.S. Gov't  3T3 Cells  JOURNAL ARTICLE

       SOURCE: National Library of Medicine.  NOTICE: This material may be
       protected by Copyright Law (Title 17, U.S.Code).

