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(Received for publication, July 10,
1995; and in revised form, November 16, 1995) Myristoylation of human immunodeficiency virus (HIV) Gag protein
is essential for virus particle budding. Two reactions are involved;
activation of free myristate to myristoyl-CoA and transfer of the
myristoyl residue to the Gag N-terminal glycine. We have investigated
the effects of triacsin C, an inhibitor of long chain acyl-CoA
synthetase, on release of HIV Gag virus-like particle (VLP) produced
using the recombinant baculovirus system. First, inhibition of acyl-CoA
formation by triacsin C was confirmed using the membrane fractions of
insect Sf9 cells as an enzyme source. Second, when HIV Gag
protein was expressed in the presence of triacsin C (0-48
µM), Gag myristoylation was inhibited in a dose-dependent
manner. Budding of Gag VLP, however, did not follow similar inhibition
kinetics but appeared unaffected up to 24 µM, yet was
completely abolished at 48 µM when the myristoylation of
Gag protein was also completely inhibited. The
``all-or-none'' inhibition of Gag VLP budding suggests that
although inhibition of acyl-CoA synthetase blocks the production of
myristoylated Gag protein, only complete inhibition of Gag
myristoylation prevents VLP budding. Thus, relatively few myristoylated
Gag molecules are sufficient for plasma membrane targeting and VLP
budding.
Volume 271,
Number 5,
Issue of February 2, 1996 pp. 2868-2873
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.
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