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M9630167.TXT
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1996-02-27
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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).