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M9480506.TXT
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1994-08-20
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Document 0506
DOCN M9480506
TI The intracytoplasmic domain of gp41 mediates polarized budding of human
immunodeficiency virus type 1 in MDCK cells.
DT 9410
AU Lodge R; Gottlinger H; Gabuzda D; Cohen EA; Lemay G; Departement de
Microbiologie et Immunologie, Universite de; Montreal, Quebec, Canada.
SO J Virol. 1994 Aug;68(8):4857-61. Unique Identifier : AIDSLINE
MED/94309148
AB Human immunodeficiency virus type 1 (HIV-1) has been shown to exhibit a
specific basolateral release in polarized epithelial cells. Previous
investigators have used vaccinia virus recombinants expressing HIV
proteins to demonstrate that virus release is nonpolarized in the
absence of viral envelope glycoproteins. In this study, we developed a
transient expression system which allows the use of Madin-Darby canine
kidney polarized epithelial cells directly grown on semipermeable
membranes. This procedure allowed us to investigate polarized HIV viral
budding following introduction of proviral DNA constructs. Expression of
env gene products in trans demonstrated the ability to polarize
env-negative viruses in a dose-dependent manner. The targeting signal
for polarized virus release was shown to be present in the envelope gp41
transmembrane protein and absent from the gp120 portion of env. At least
part of this signal is within the gp41 intracytoplasmic domain. Mutants
of the p17gag matrix protein were shown to be nonpolarized only when
unable to interact with the envelope glycoproteins. Together, these data
are consistent with a model of polarized virus budding in which capsid
proteins, lacking a targeting signal, are targeted for specific
basolateral release via an interaction of p17 with the envelope
glycoprotein containing the polarization signal in its intracytoplasmic
domain.
DE Animal Biological Transport Cell Line Cloning, Molecular
Cytoplasm/METABOLISM Dogs Gene Products, env/PHYSIOLOGY Gene
Products, gag/GENETICS/METABOLISM HIV Antigens/GENETICS/METABOLISM HIV
Envelope Protein gp41/GENETICS/*PHYSIOLOGY HIV-1/*PHYSIOLOGY Mutation
Protein Precursors/PHYSIOLOGY Signal Peptides/METABOLISM Support,
Non-U.S. Gov't Support, U.S. Gov't, P.H.S. Virus Replication JOURNAL
ARTICLE
SOURCE: National Library of Medicine. NOTICE: This material may be
protected by Copyright Law (Title 17, U.S.Code).