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J. Biol. Chem., Vol. 275, Issue 21, 15809-15819, May 26, 2000
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From the We previously demonstrated that an
envelope mutant of human immunodeficiency virus type 1 lacking the
entire cytoplasmic domain interferes in trans with the
production of infectious virus by inclusion of the mutant envelope into
the wild-type envelope complex. We also showed that the envelope
incorporation into virions is not affected when the wild-type envelope
is coexpressed with the mutant envelope. These results suggest that an
oligomeric structure of the cytoplasmic domain is functionally required
for viral infectivity. To understand whether the cytoplasmic domain of
human immunodeficiency virus type 1 transmembrane protein gp41 has the
potential to self-assemble as an oligomer, in the present study we
fused the coding sequence of the entire cytoplasmic domain at 3' to the
Escherichia coli malE gene, which encodes a monomeric
maltose-binding protein. The expressed fusion protein was examined by
chemical cross-linking, sucrose gradient centrifugation, and gel
filtration. The results showed that the cytoplasmic domain of gp41
assembles into a high-ordered structural complex. The intersubunit
interaction of the cytoplasmic domain was also confirmed by a mammalian
two-hybrid system that detects protein-protein interactions in
eucaryotic cells. A cytoplasmic domain fragment expressed in eucaryotic
cells was pulled down by glutathione-Sepharose 4B beads via its
association with another cytoplasmic domain fragment fused to the C
terminus of the glutathione S-transferase moiety. We also
found that sequences encompassing the lentiviral lytic peptide-1 and
lentiviral lytic peptide-2, which are located within residues 828-856
and 770-795, respectively, play a critical role in cytoplasmic domain
self-assembly. Taken together, the results from the present study
indicate that the cytoplasmic domain of gp41 by itself is sufficient to
assemble into a multimeric structure. This finding supports the
hypothesis that a multimeric form of the gp41 cytoplasmic domain plays
a crucial role in virus infectivity.
Multimerization Potential of the Cytoplasmic Domain of the Human
Immunodeficiency Virus Type 1 Transmembrane Glycoprotein gp41*
,,,, and¶
Division of Infectious Diseases, Institute
of Biomedical Sciences, Academia Sinica, Taipei 11529, Taiwan, Republic
of China and § Institute of Clinical Medicine, National
Yang-Ming University, School of Medicine, and Department of Medical
Research and Education, Taipei Veterans General Hospital, Taipei 11217, Taiwan, Republic of China
*
This work was supported by Department of Health Grants
DOH87-TD-1035 and DOH88-TD-1085 and the National Science Council Grant 89-2320-B-001-019) and by grants from the Institute of Biomedical Sciences at Academia Sinica (Taipei, Taiwan, Republic of China).The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
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