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1996-02-26
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Document 1036
DOCN M9621036
TI Single basic amino acid substitutions at position 302 or 320 in the V3
domain of HIV type 1 are not sufficient to alter the antiviral activity
of dextran sulfate and heparin.
DT 9602
AU Okada T; Gurney ME; Department of Cell, Molecular, and Structural
Biology,; Northwestern University Medical School, Chicago, Illinois
60611,; USA.
SO AIDS Res Hum Retroviruses. 1995 May;11(5):571-5. Unique Identifier :
AIDSLINE MED/96093892
AB The third variable domain (V3 domain) of the human immunodeficiency
virus type 1 (HIV-1) envelope glycoprotein gp120 contains a substantial
number of positively charged amino acid residues. We previously
demonstrated that mutation of basic amino acid residues at position 303,
306, 309, 313, and 325 in the V3 domain of HIV-1 strain NL4-3 resulted
in a dramatic elimination of both virus infectivity and
syncytium-inducing ability. Mutations of arginine at position 302 to
serine (R302S) or lysine at position 320 to glutamine (K320Q) had
variable effects on infectivity for a panel of T cell lines tested.
These mutations are located on opposite sides of the Gly-Pro-Gly-Arg-Ala
sequence in the center of the V3 domain. The R302S and K320Q mutations
allowed us to determine if these basic residues are important for virus
neutralization by polyanionic compounds. Dextran sulfate and heparin
inhibited the cytopathogenicities of both mutants for MT-4 cells,
although their 50% antiviral effective doses were slightly higher than
those required to achieve complete protection against wild-type
HIV-1NL4-3 replication. This result emphasizes that the basic amino
acids of Arg302 and Lys320 are not essential for the inhibitory effect
of dextran sulfate and heparin on HIV-1 infection.
DE Amino Acid Sequence Antiviral Agents/*PHARMACOLOGY Arginine/GENETICS
Base Sequence Cell Line Dextran Sulfate/*PHARMACOLOGY DNA Primers
Electrochemistry Glutamine/GENETICS Heparin/*PHARMACOLOGY Human HIV
Envelope Protein gp120/CHEMISTRY/*DRUG EFFECTS/GENETICS HIV-1/*DRUG
EFFECTS/GENETICS Lysine/GENETICS Molecular Sequence Data Mutagenesis,
Site-Directed Peptide Fragments/CHEMISTRY/*DRUG EFFECTS/GENETICS
Serine/GENETICS Support, Non-U.S. Gov't Support, U.S. Gov't, P.H.S.
JOURNAL ARTICLE
SOURCE: National Library of Medicine. NOTICE: This material may be
protected by Copyright Law (Title 17, U.S.Code).