       Document 0167
 DOCN  M9630167
 TI    A synthetic peptide corresponding to a conserved heptad repeat domain is
       a potent inhibitor of Sendai virus-cell fusion: an emerging similarity
       with functional domains of other viruses.
 DT    9603
 AU    Rapaport D; Ovadia M; Shai Y; Department of Membrane Research and
       Biophysics, Weizmann; Institute of Science, Rehovot, Israel.
 SO    EMBO J. 1995 Nov 15;14(22):5524-31. Unique Identifier : AIDSLINE
       MED/96091124
 AB    A series of peptides derived from three domains within the fusion
       protein of Sendai virus was synthesized and examined for their potential
       to inhibit the fusion of the virus with human red blood cells. These
       domains include the 'fusion peptide' and two heptad repeats, one
       adjacent to the fusion peptide (SV-163) and the other to the
       transmembrane domain (SV-473). Of all the peptides tested, only SV-473
       was highly inhibitive. Using fluorescently-labelled peptides, the
       mechanism through which the SV-473 peptide inhibits the haemolytic
       activity of the virus was investigated. The results suggest that
       interactions of the active peptide with virion elements and lipid
       membranes are involved. Since it has recently been found that synthetic
       peptides corresponding to putative coiled-coil domains of the human
       immunodeficiency virus (HIV) type 1 transmembrane protein gp41 are
       potent inhibitors of HIV, we discuss the general property of
       virus-derived coiled-coil peptides as inhibitors of viral infection.
 DE    Amino Acid Sequence  Animal  Binding Sites  Chick Embryo  *Conserved
       Sequence  Erythrocyte Membrane/VIROLOGY  Human  *Membrane Fusion/DRUG
       EFFECTS  Molecular Sequence Data  Parainfluenza Virus Type 1/*DRUG
       EFFECTS/METABOLISM/PATHOGENICITY  Peptides/CHEMICAL
       SYNTHESIS/*PHARMACOLOGY  Repetitive Sequences, Nucleic Acid  Support,
       Non-U.S. Gov't  Viral Fusion Proteins/CHEMICAL SYNTHESIS/*PHARMACOLOGY
       JOURNAL ARTICLE

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

