![[Feedback]](/icons/banner/feedbackACT.gif)
![[For Subscribers]](/icons/banner/subscriberACT.gif)
![[Archive]](/icons/banner/archiveACT.gif)
![[Search]](/icons/banner/searchACT.gif)
![[Contents]](/icons/banner/tocACT.gif)
Previous Article | Next Article 
Journal of Virology, December 1999, p. 10508-10513, Vol. 73, No. 12
0022-538X/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.
Cellular Motor Protein KIF-4 Associates with
Retroviral Gag
Yao
Tang,1
Ulrike
Winkler,1
Eric O.
Freed,2
Ted A.
Torrey,1
Wankee
Kim,3
Henry
Li,4
Stephen P.
Goff,4 and
Herbert C.
Morse III1,*
Laboratory of
Immunopathology1 and Laboratory of
Molecular Microbiology,2 National Institute of
Allergy and Infectious Diseases, National Institutes of Health,
Bethesda, Maryland 20892; Institute for Medical Science,
School of Medicine, Ajou University, Suwon,
Korea3; and Department of Biochemistry
and Molecular Biophysics, Columbia University College of Physicians
and Surgeons, New York, New York4
Received 26 March 1999/Accepted 24 August 1999
 |
ABSTRACT |
Previously we demonstrated that murine retroviral Gag proteins
associate with a cellular motor protein, KIF-4. Using the yeast two-hybrid assay, we also found an association of KIF-4 with Gag proteins of Mason-Pfizer monkey virus (MPMV), simian immunodeficiency virus (SIV), and human immunodeficiency virus type 1 (HIV-1). Studies
performed with mammalian cell systems confirmed that the HIV-1 Gag
protein associates with KIF-4. Soluble cytoplasmic proteins from cells
infected with recombinant vaccinia virus expressing the entire Gag-Pol
precursor protein of HIV-1 or transfected with HIV-1 molecular clone
pNL4-3 were fractionated by sucrose gradient centrifugation and further
separated by size-exclusion and anion-exchange chromatographies. KIF-4
and HIV-1 Gag cofractionated in both chromatographic separations.
Immunoprecipitation assays have also verified the KIF-4-Gag
association. KIF-4 binds mainly to the Gag precursor (Pr55 Gag) and a
matrix-capsid processing intermediate (Pr42) but not to other processed
Gag products. The binding of Gag is mediated by a domain of KIF-4
proximal to the C terminus. These results, and our previous studies,
raise the possibility that KIF-4 may play an important role in
retrovirus Gag protein transport.
| |
TEXT |
A key step in the retroviral
replication cycle involves a process in which a large number of
chemically distinct macromolecules are transported through different
pathways to the plasma membrane of the cell, where they are assembled
into nascent viral particles. The internal protein shell or capsid of
the virus is assembled from a large number of
polyprotein precursors that must be
transported through the cytoplasm
either preassembled, in small
groups, or as monomersto the inner face of the plasma membrane. The
Gag protein of retroviruses directs the assembly and release of
virus-like particles from the cell even when expressed in the absence
of all other virus-encoded components (12). Several
mechanisms of Gag transport have been suggested: (i) free diffusion
from the cytoplasm to the cell membrane, (ii) interaction with elements of the cytoskeletal system (2), or (iii) binding to the
outer surface of the Golgi apparatus and then trafficking to the plasma membrane on transport vesicles (7). The actual mechanism by which Gag polyproteins arrive at the plasma membrane remains unclear.
View larger version (41K):
[in this window]
[in a new window]
|
FIG. 1.
Binding domain for KIF-4 in MMLV Gag in YTHS. Gal4AD-Y26
was used as bait to interact against different Gag domains fused with
Gal4DB. CA, capsid; NC, nucleocapsid; WT, wild-type; MHR, major
homology region.
|
|
KIF-4 was identified as a cellular motor protein that belongs to the
kinesin superfamily (11). Structurally, it has three domains: an NH2-terminal globular motor, a central
-helical stalk, and the COOH-terminal tail. This protein is
expressed in all cell lines and mouse tissues tested (6).
The intracellular localization of KIF-4 as determined by
immunocytochemistry and subcellular fractionation suggests that nearly
50% of KIF-4 is located in the nucleus, while the rest associates with
membranous organelles (11). Recent studies have demonstrated
that about 25% of cytoplasmic KIF-4 is associated with
mitochondria in human immunodeficiency virus type 1 (HIV-1)transfected cell lines (13). It has been suggested that KIF-4 is a microtubule plus end-directed motor for
transport of a certain group of membranous organelles in juvenile neurons and other cells (11). The function of KIF-4,
however, is not fully understood.
Our previous studies showed that a C-terminal portion of KIF-4,
designated Y26, interacts with murine leukemia virus (MuLV) Gag
proteins in the yeast two-hybrid system (YTHS) and in MuLV-infected cells (6). Here we show that this domain also binds to
HIV-1, simian immunodeficiency virus (SIV), Mason-Pfizer monkey virus (MPMV), and Rous sarcoma virus (RSV) Gag proteins in the YTHS and
present detailed studies of the KIF-4-HIV-1 Gag association. The data
suggest that KIF-4 may play a role as a molecular motor for Gag transport.
KIF-4 binds multiple retrovirus Gag polyproteins in the YTHS.
The C-terminal portion of KIF-4, isolated previously as a Gal4AD fusion
clone (designated Gal4AD-Y26), was used as bait to interact against
multiple Gag polyproteins, including those of HIV-1, SIV, MPMV, RSV,
and Moloney MuLV (MMLV). The respective gag genes were
cloned into pMA424 and fused with the Gal4 DNA-binding domain
(Gal4DBD-Gag) for analysis in the YTHS as described before (1, 3,
9). We found that KIF-4 interacted strongly with all full-length
Gag proteins (Table 1). This result
confirms and extends our previous studies that showed that KIF-4-Gag
association could be detected by coimmunoprecipitation in cells
infected with different classes of MuLV (6). To map the
binding site of KIF-4 to Gag, MMLV Gag fragments were amplified by PCR
as a single domain or as combinations of domains (Fig. 1) and cloned
into the pSH2-1 vector encoding fusion with the LexADBD binding domain.
We found that the KIF-4 binding site of MMLV Gag is located in matrix
(MA) (Fig. 1). An identical result was obtained when pGBT9 was used as
a vector for Gag domain fusion constructs (data not shown).
The MA domain of Gag plays a crucial role in retrovirus assembly and
budding by virtue of myristylation and resulting plasma membrane
association, although myristylation itself is not sufficient for plasma
membrane binding (4). It is not clear when Gag binds to the
cytoplasmic membrane, but the finding that MA associates with KIF-4
could point to a mechanism for Gag polyprotein transport from the
cytoplasm to the inner face of the cell membrane.
Identification and characterization of KIF-4-HIV-1 Gag association
in vivo.
The association of KIF-4 and HIV-1 Gag proteins was
examined further by using the procedures outlined in the flow chart
shown in Fig. 2. HeLa cells (5 × 106/75-cm2 flask) were plated and cultured
overnight in Dulbecco's modified Eagle's medium (DMEM) (Quality
Biological, Inc., Gaithersburg, Md.) with 5% fetal bovine serum. The
next day, the cells were washed twice with serum-free medium and
infected with the HIV-1-expressing vaccinia virus vector vVK
(5), kindly provided by Bernard Moss (Laboratory of Viral
Diseases, National Institute of Allergy and Infectious Disease,
National Institutes of Health). The vVK virus stock was diluted in
serum-free medium to a concentration of 0.02 PFU/cell and incubated
with HeLa cells at 37°C for 1 h. The cells were then cultured in
5% fetal bovine serum-DMEM medium (without washing away the virus)
for another 48 to 72 h for maximum cytopathic effect. The cells
were harvested by gently scraping them from the flask, washed twice in
H-S buffer (10 mM HEPES, 0.5 M NaCl [pH 7.2]), and then resuspended
in 2 ml of H-S buffer containing 6% sucrose and protease inhibitors
(COMPLETE Mini; Boehringer Mannheim, Indianapolis, Ind.). Sonication
was performed in a tank-type sonicator for 10 s/run until more than
80% of the cells were broken as determined microscopically. Unbroken
cells and nuclei were removed by centrifugation at 1,200 × g for 5 min to obtain a postnuclear fraction. All procedures were
performed on ice or at 4°C to prevent proteolysis.
The postnuclear fraction (2 ml) was loaded onto a sucrose
equilibrium-density gradient, which was prepared by layering 1.5 ml of
each stock sucrose solution (from 60 to 10%, bottom to top, in 10%
increments) and equilibration for 24 h at 4°C. The gradients were then ultracentrifuged in an SW41 rotor (Beckman, Columbia, Md.) at
35,000 rpm for 22 h at 4°C. Fractions (0.5 ml) were aspirated from the bottom to the top. Protein concentrations were measured with a
bicinchoninic acid protein detection kit (Pierce, Rockford, Ill.) (Fig.
3A). Western blot analyses, performed as
described previously (6), were used to detect fractions
containing KIF-4 and HIV-1 Gag. Polyclonal anti-KIF4 (11)
and monoclonal anti-HIV-1 P24 antibodies (NIH AIDS Research and
Reference Reagent Program, Rockville, Md.) were the detecting reagents.
Among the 21 fractions, most of HIV-1 Gag protein was seen in fractions
14 to 21, with a peak at fractions 14 to 17 in the density range of
1.05 to 1.08 (Fig. 3B). The Gag-Pol Pr160 was seen in fractions 13 to
16, colocalized with the peak of Pr55 and Pr42 (MA-capsid). A small
amount of Gag was also detected in fractions 4 to 8 (density, 1.15 to
1.17) with Gag precursor Pr55 and small amounts of Pr42 and P24 (data not shown). The full-length KIF-4 protein (140 kDa) colocalized with
Pr55 in fractions 14 to 17 (Fig. 3C).
View larger version (56K):
[in this window]
[in a new window]
|
FIG. 3.
Sucrose gradient fractionation of postnuclear
supernatants from vVK-infected HeLa cells. (A) Protein density versus
total protein concentration; (B and C) Western blotting of each
fraction with anti-HIV-1 Gag Pr24 (B) and anti-KIF-4 (C). PN,
postnuclear cell lysate.
|
|
A recent study described two forms of putative Gag assembly
intermediates in HIV-1-infected CD4+ T cells,
HIV-1-infected SupT-1 and Jurkat cells, and HIV-1-transfected HeLa and
COS cellsa detergent-resistant complex and a detergent-sensitive complex (8). The density of the intermediates was determined as 1.10 to 1.13 for the detergent-resistant complex (containing mostly
Pr55 and Pr160Gag-Pol precursors) and 1.15 to 1.17 for the
detergent-sensitive complex, which is similar to the density of mature
HIV-1 virions. Our sucrose gradient study also identified two complexes
with different densities that shared similar Gag and Pol components as
in the referenced study. We note that the densities of both complexes
in our results are lower than those reported (8), possibly
due to experimental differences.
To examine whether the complex containing both KIF-4 and Gag proteins
can be further separated biochemically, we used size-exclusion and
ion-exchange chromatographies. Fractions 14 to 16 from the sucrose
gradient separation, which were positive for both KIF-4 and HIV-1 Gag
proteins by Western blot analysis (Fig. 3), were pooled and diluted 1:1
in the running buffers for chromatography.
For separating proteins by size, we used a Bio-Prep column 1000/17
(Bio-Rad Laboratories, Hercules, Calif.) that generates linear
fractionation from 10 to 1,000 kDa. A total of 0.5 mg of soluble
protein in 0.3 ml of H-S running buffer was loaded, and the running
procedure was performed under the Bio-Logic System (Bio-Rad) with a
flow rate of 0.5 ml/min. Forty-one fractions of 0.5 ml were collected
and pooled into eight groups according to the distribution of the peaks
shown in Fig. 4A. Protein pellets obtained by ultracentrifugation with a Beckman SW50.1 rotor at 40,000 rpm for 1 h at 4°C were suspended in 1× sample buffer, boiled,
and loaded onto 12% polyacrylamide-Tris-glycine gels (Novex Experimental Technology, San Diego, Calif.) for Western blotting. Figure 4B shows that the majority of HIV-1 Gag protein is present in
group 5 and a small amount is present in groups 2 and 4. There is more
Pr42 and less Pr55 in group 5 but more Pr55 than Pr42 in groups 2 and
4. No additional processed Gag proteins were detected in any groups.
Full-length KIF-4 proteins were mainly recovered in group 5 (Fig. 4C),
in which the majority of Pr42 was present. A small amount of
full-length KIF-4 was also detected in group 4, where mainly Pr55 was
found. Some small bands reacting with anti-KIF-4 antibody can be seen
in groups 5, 7, and 8. They probably represent either processed or
degraded KIF-4 molecules. A postnuclear fraction from uninfected HeLa
cells was also examined. KIF-4 eluted one or two fractions ahead of its
position in material from infected cells (data not shown).
View larger version (40K):
[in this window]
[in a new window]
|
FIG. 4.
Size-exclusion chromatography analysis of vVK-infected
HeLa cells. Fractions 14 to 17 from sucrose gradient separation were
pooled and passed through a 1000/17 column. (A) Histogram of protein
distribution in each fraction and grouping of fractions according to
elution peaks of protein; (B and C) Western blot analysis of each group
with anti-HIV-1 Gag Pr24 monoclonal antibody (B) and anti-KIF-4
antibody (C). PN, postnuclear cell lysate; OD280, optical
density at 280 nm.
|
|
Separation of proteins by their surface charge was accomplished with
ion-exchange chromatography using a UNO Q-1 column (Bio-Rad) in
accordance with the manufacturer's directions. A total of 0.5 mg of
soluble protein in a total of 0.5 ml was loaded onto the column. The
running buffer was started with 20 mM Tris (buffer A, pH 8.2), followed
by increasing concentrations of buffer B (20 mM Tris plus 1.0 M NaCl
[pH 8.2]) to elute the proteins. Eighteen fractions were collected
(Fig. 5A). The majority of Gag Pr55 and Pr42 proteins were recovered in fractions 9 to 18, with a peak around
fractions 10 to 15 (Fig. 5B). Substantial amounts of Pr42 and some Pr24
were eluted in fractions 6 to 9 at lower salt concentrations. Full-length KIF-4 protein was present in fractions 11 to 16 (Fig. 5C),
which corresponds to the peak concentration of full-length Gag and
Pr42. Smaller anti-KIF-4 antibody-reactive bands of 70 and 35 kDa were
also detected in fractions 7 to 9 and 13 to 15, respectively. The
35-kDa band was consistently detected in vVK-infected cells but not in
cells infected by other viruses, suggesting that a vaccinia protease
may cut KIF-4 to yield a 35-kDa fragment. A very small amount of Pr24
protein was detected in fractions 4 and 5, which could be caused by a
further proteolysis of Gag during separation. The full-length KIF-4
protein, however, was always associated with Pr55 and Pr42 Gag
proteins. Similar results were obtained in two further studies using
vVK-infected HeLa cells and in two analyses of vVK-infected BHK 21 cells. The fact that a KIF-4-HIV Gag complex in vVK-infected
postnuclear supernatant remained intact during chromatographic
separations following sucrose density fractionation suggests that the
association between KIF-4 and Gag proteins is fairly stable. It is not
known whether other cellular proteins are required for this
association.
View larger version (65K):
[in this window]
[in a new window]
|
FIG. 5.
Anion-exchange chromatography analysis of vVK-infected
HeLa cells. Fractions 14 to 17 from sucrose gradient separation were
pooled and passed through an UNO Q-1 column. (A) Histogram of protein
distribution in each fraction with salt concentration (20 mM Tris or 20 mM Tris plus 1.0 M NaCl; dotted line) and conductivity (solid line)
during separation; (B and C) Western blot analysis with anti-HIV-1 Pr24
Gag (B) and anti-KIF-4 (C). PN, postnuclear cell lysate;
OD280, optical density at 280 nm.
|
|
Identification of KIF-4-HIV-1 Gag association by
coimmunoprecipitation.
Immunoprecipitation studies with both
anti-HIV-1 serum and anti-KIF-4-conjugated beads were used to study the
KIF-4-Gag association in either vVK-infected HeLa cells or HeLa cells
transfected with the pNL4-3 HIV-1 proviral clone. Briefly, cells were
plated at 106/60-mm dish and were transfected the next day
with 25 µg of proviral DNA per dish. Transfected cells were cultured
for another 2 days before lysing.
Affinity-purified anti-mouse KIF-4 polyclonal antibody (11),
which cross-reacts with KIF-4s in human, monkey, and hamster cells
(data not shown), was conjugated to Sepharose 4B beads (6). Human HIV-1-positive serum (NIH AIDS Research and Reference Reagent Program) was conjugated to immobilized protein A-agarose beads (Pierce)
at a concentration of 1 mg/ml of beads. Y26 was expressed as a
glutathione S-transferase (GST) fusion protein and
conjugated to Sepharose 4B beads as described previously
(6).
After incubation of the postnuclear fraction of vVK-infected HeLa cells
with anti-KIF-4 antibody-conjugated beads or GST-Y26 fusion
protein-bound beads, Pr55 Gag, but not processed Gag, was found to
coprecipitate (Fig. 6, lanes 4 and 5). In
contrast, no KIF-4 was detected after precipitation with anti-HIV-1
beads (Fig. 6, lane 2). Lane 3 shows the Gag proteins in the
postnuclear supernatant, and lane 1 is a positive control for KIF-4 in
the lysate after anti-KIF-4 bead precipitation. It has always been more
difficult to bring down KIF-4 with anti-HIV-1 antibodies, either
monoclonal or polyclonal, than to coprecipitate Gag proteins with
anti-KIF-4 antibody by using lysates of vVK-infected or
pNL4-3-transfected cells.
View larger version (45K):
[in this window]
[in a new window]
|
FIG. 6.
Coimmunoprecipitation analyses of vVK-infected HeLa
cells. Antibody-conjugated beads, anti-KIF-4 on Sepharose 4B (lanes 1 and 4) or anti-HIV-1 on protein A beads (lane 2), and GST-Y26 fusion
protein on Sepharose (lane 5) were incubated with a postnuclear
fraction of vVK-infected HeLa cells. Blots were developed with either
anti-KIF-4 polyclonal antibody (left two lanes) or anti-HIV-1 Pr24 Gag
monoclonal antibodies (right three lanes). Lane 3 is a positive control
for Gag in the postnuclear fraction of vVK-infected HeLa cells.
|
|
Our previous studies of MuLV-infected cells also showed that only a
small portion of KIF-4 and Gag proteins are bound to each other
(6). The results described above suggest that the beads conjugated with anti-HIV-1 or anti-Gag antibodies could primarily react
with "free Gag," resulting in a much reduced chance for the
KIF-4-Gag complex to be pulled down during immunoprecipitation, especially in cell lines that overexpress Gag protein. On the other
hand, the precipitation with anti-KIF-4 antibody has a better chance to
bring down Gag proteins because the limited amount of cytoplasmic KIF-4
could allow KIF-4-Gag complex to bind to the antibody-conjugated beads.
Purified HIV-1 particles from pNL4-3-transfected or vVK-infected HeLa
cells, and other sources (10), were lysed with NP-40 and
incubated with beads to see whether KIF-4 is present in mature virions.
No full-length KIF-4 species were found, although smaller bands that
interact with anti-KIF-4 antibody could be seen by direct Western blot
analysis or after immunoprecipitation (data not shown). Again, the
significance of the smaller KIF-4 fragments in KIF-4-Gag association
is unclear.
In summary, our studies have shown that the cellular motor protein
KIF-4 associates with a number of Gag proteins, including HIV-1 Gag.
This association was initially observed in the YTHS and confirmed in
mammalian cells by cell fractionation, chromatography, and
coimmunoprecipitation studies. KIF-4 has been described as a cellular
motor protein that may transport cytoplasmic proteins or vesicles to
the cell membrane. Our data now raise the possibility that KIF-4 may be
involved in the transport of Gag proteins in retrovirus-infected cells.
| |
ACKNOWLEDGMENTS |
We thank Yasushi Okada, Nobutaka Hirokawa, and Bruce Chesebro for
antibodies and Brenda Rae Marshall for excellent editorial assistance.
This work was funded in part by a grant from the Intramural
AIDS-Targeted Antiviral Program. W.K. was supported by nondirected research funds from the Korean Research Foundation, 1996. S.P.G. is an
Investigator of the Howard Hughes Medical Institute.
| |
FOOTNOTES |
*
Corresponding author. Mailing address: LIP,
NIAID, NIH, Building 7, Room 304, MSC 0760, Bethesda, MD 20892-0760. Phone: (301) 496-6379. Fax: (301) 402-0077. E-mail:
hm16c{at}nih.gov.
| |
REFERENCES |
| 1.
|
Alin, K., and S. P. Goff.
1996.
Mutational analysis of interactions between the Gag precursor proteins of murine leukemia viruses.
Virology
216:418-424[Medline].
|
| 2.
|
Edbauer, C. A., and R. B. Naso.
1983.
Cytoskeleton-associated Pr65gag and retrovirus assembly.
Virology
130:415-426[Medline].
|
| 3.
|
Franke, E. K.,
H. E. H. Yuan,
K. L. Bossolt,
S. P. Goff, and J. Luban.
1994.
Specificity and sequence requirements for interactions between various retroviral Gag proteins.
J. Virol.
68:5300-5305[Abstract/Free Full Text].
|
| 4.
|
Freed, E. O., and M. A. Martin.
1995.
Virion incorporation of envelope glycoproteins with long but not short cytoplasmic tails is blocked by specific, single amino acid substitutions in the human immunodeficiency virus type 1 matrix.
J. Virol.
69:1984-1989[Abstract].
|
| 5.
|
Karacostas, V.,
K. Nagashima,
M. A. Gonda, and B. Moss.
1989.
Human immunodeficiency virus-like particles produced by a vaccinia virus expression vector.
Proc. Natl. Acad. Sci. USA
86:8964-8967[Abstract/Free Full Text].
|
| 6.
|
Kim, W. K.,
Y. Tang,
Y. Okada,
T. A. Torrey,
S. K. Chattopadhyay,
M. Pfleiderer,
F. G. Falkner,
F. Dorner,
W. Choi,
N. Hirokawa, and H. C. Morse, III.
1998.
Binding of murine leukemia virus Gag polyproteins to KIF-4, a microtubule-based motor protein.
J. Virol.
72:6898-6901[Abstract/Free Full Text].
|
| 7.
|
Krausslich, J. G., and R. Welker.
1996.
Intracellular transport of retroviral capsid components.
Curr. Top. Microbiol. Immunol.
214:25-63[Medline].
|
| 8.
|
Lee, Y. M., and X. F. Yu.
1998.
Identification and characterization of virus assembly intermediate complexes in HIV-infected CD4+ T cells.
Virology
243:78-93[Medline].
|
| 9.
|
Li, A.,
B. Yuan, and S. P. Goff.
1997.
Genetic analysis of interactions between Gag proteins of Rous sarcoma virus.
J. Virol.
71:5624-5630[Abstract].
|
| 10.
|
Ott, D. E.,
L. V. Coren,
B. P. Kane,
L. K. Bush,
D. G. Johnson,
R. C. Sowder II,
E. N. Chertova,
L. O. Arthur, and L. E. Henderson.
1996.
Cytoskeletal proteins inside human immunodeficiency virus type 1 virions.
J. Virol.
70:7734-7743[Abstract].
|
| 11.
|
Sekine, Y.,
Y. Okada,
Y. Noda,
S. Kondo,
H. Aizawa,
R. Takemura, and N. Hirokawa.
1994.
A novel microtubule-based motor protein (KIF-4) for organelle transports, whose expression is regulated developmentally.
J. Cell Biol.
127:187-201[Abstract/Free Full Text].
|
| 12.
|
Wills, J. W., and R. C. Craven.
1991.
Form, function, and use of retroviral Gag proteins.
AIDS
5:639-654[Medline].
|
| 13.
| Winkler, U. Unpublished data.
|
Journal of Virology, December 1999, p. 10508-10513, Vol. 73, No. 12
0022-538X/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.
This article has been cited by other articles:
-
Yi, C.-r., Rosenberg, N.
(2008). Mutations Affecting the MA Portion of the v-Abl Protein Reveal a Conserved Role of Gag in Abelson Murine Leukemia Virus (MLV) and Moloney MLV. J. Virol.
82: 5307-5315
[Abstract]
[Full Text]
-
Jin, J., Sturgeon, T., Chen, C., Watkins, S. C., Weisz, O. A., Montelaro, R. C.
(2007). Distinct Intracellular Trafficking of Equine Infectious Anemia Virus and Human Immunodeficiency Virus Type 1 Gag during Viral Assembly and Budding Revealed by Bimolecular Fluorescence Complementation Assays. J. Virol.
81: 11226-11235
[Abstract]
[Full Text]
-
Swanson, I., Jude, B. A., Zhang, A. R., Pucker, A., Smith, Z. E., Golovkina, T. V.
(2006). Sequences within the gag Gene of Mouse Mammary Tumor Virus Needed for Mammary Gland Cell Transformation.. J. Virol.
80: 3215-3224
[Abstract]
[Full Text]
-
Beriault, V., Clement, J.-F., Levesque, K., LeBel, C., Yong, X., Chabot, B., Cohen, E. A., Cochrane, A. W., Rigby, W. F. C., Mouland, A. J.
(2004). A Late Role for the Association of hnRNP A2 with the HIV-1 hnRNP A2 Response Elements in Genomic RNA, Gag, and Vpr Localization. J. Biol. Chem.
279: 44141-44153
[Abstract]
[Full Text]
-
Jouvenet, N., Monaghan, P., Way, M., Wileman, T.
(2004). Transport of African Swine Fever Virus from Assembly Sites to the Plasma Membrane Is Dependent on Microtubules and Conventional Kinesin. J. Virol.
78: 7990-8001
[Abstract]
[Full Text]
-
Hemonnot, B., Cartier, C., Gay, B., Rebuffat, S., Bardy, M., Devaux, C., Boyer, V., Briant, L.
(2004). The Host Cell MAP Kinase ERK-2 Regulates Viral Assembly and Release by Phosphorylating the p6gag Protein of HIV-1. J. Biol. Chem.
279: 32426-32434
[Abstract]
[Full Text]
-
Petit, C., Giron, M.-L., Tobaly-Tapiero, J., Bittoun, P., Real, E., Jacob, Y., Tordo, N., de The, H., Saib, A.
(2003). Targeting of incoming retroviral Gag to the centrosome involves a direct interaction with the dynein light chain 8. J. Cell Sci.
116: 3433-3442
[Abstract]
[Full Text]
-
Liu, M., Li, X.-L., Hassel, B. A.
(2003). Proteasomes Modulate Conjugation to the Ubiquitin-like Protein, ISG15. J. Biol. Chem.
278: 1594-1602
[Abstract]
[Full Text]
-
Sodeik, B.
(2002). Unchain my heart, baby let me go--the entry and intracellular transport of HIV. J. Cell Biol.
159: 393-395
[Abstract]
[Full Text]
-
Myers, E. L., Allen, J. F.
(2002). Tsg101, an Inactive Homologue of Ubiquitin Ligase E2, Interacts Specifically with Human Immunodeficiency Virus Type 2 Gag Polyprotein and Results in Increased Levels of Ubiquitinated Gag. J. Virol.
76: 11226-11235
[Abstract]
[Full Text]
-
Serhan, F., Jourdan, N., Saleun, S., Moullier, P., Duisit, G.
(2002). Characterization of Producer Cell-Dependent Restriction of Murine Leukemia Virus Replication. J. Virol.
76: 6609-6617
[Abstract]
[Full Text]
-
Gurer, C., Cimarelli, A., Luban, J.
(2002). Specific Incorporation of Heat Shock Protein 70 Family Members into Primate Lentiviral Virions. J. Virol.
76: 4666-4670
[Abstract]
[Full Text]
-
Le Blanc, I., Blot, V., Bouchaert, I., Salamero, J., Goud, B., Rosenberg, A. R., Dokhelar, M.-C.
(2002). Intracellular Distribution of Human T-Cell Leukemia Virus Type 1 Gag Proteins Is Independent of Interaction with Intracellular Membranes. J. Virol.
76: 905-911
[Abstract]
[Full Text]
-
Bacharach, E., Gonsky, J., Alin, K., Orlova, M., Goff, S. P.
(2000). The Carboxy-Terminal Fragment of Nucleolin Interacts with the Nucleocapsid Domain of Retroviral Gag Proteins and Inhibits Virion Assembly. J. Virol.
74: 11027-11039
[Abstract]
[Full Text]
-
Mouland, A. J., Mercier, J., Luo, M., Bernier, L., DesGroseillers, L., Cohen, E. A.
(2000). The Double-Stranded RNA-Binding Protein Staufen Is Incorporated in Human Immunodeficiency Virus Type 1: Evidence for a Role in Genomic RNA Encapsidation. J. Virol.
74: 5441-5451
[Abstract]
[Full Text]
Top
Abstract
Text
