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Journal of Virology, April 2000, p. 3548-3554, Vol. 74, No. 8
Laboratory of Molecular Microbiology,
National Institute of Allergy and Infectious Diseases, National
Institutes of Health, Bethesda, Maryland 20892-0460
Received 14 December 1999/Accepted 26 January 2000
The incorporation of envelope (Env) glycoproteins into virions is
an essential step in the retroviral replication cycle. Lentiviruses, including human immunodeficiency virus type 1 (HIV-1), encode Env
glycoproteins with unusually long cytoplasmic tails, the functions of
which have not been fully elucidated. In this study, we examine the
effects on virus replication of a number of mutations in a helical
motif (
0022-538X/00/$04.00+0
Genetic Evidence for an Interaction between Human
Immunodeficiency Virus Type 1 Matrix and
-Helix 2 of the gp41
Cytoplasmic Tail
-helix 2) located near the center of the HIV-1 gp41
cytoplasmic tail. We find that, in T-cell lines, small deletions in
this domain disrupt the incorporation of Env glycoproteins into virions
and markedly impair virus infectivity. Through the analysis of viral
revertants, we demonstrate that a single amino acid change (34VI) in
the matrix domain of Gag reverses the Env incorporation and infectivity
defect imposed by a small deletion near the C terminus of
-helix 2. These results provide genetic evidence, in the context of infected T
cells, for an interaction between HIV-1 matrix and the gp41
cytoplasmic tail and identify domains of both proteins involved in this
putative interaction.
*
Corresponding author. Mailing address: Bldg. 4, Rm.
307, NIAID, NIH, Bethesda, MD 20892-0640. Phone: (301) 402-3215. Fax: (301) 402-0226. E-mail: EFreed{at}nih.gov.
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