Effects of human immunodeficiency virus type 1 transframe protein p6* mutations on viral protease-mediated Gag processing.

@article{Chiu2006EffectsOH,
  title={Effects of human immunodeficiency virus type 1 transframe protein p6* mutations on viral protease-mediated Gag processing.},
  author={Hsu-Chen Chiu and Fujiang Wang and Yi-Ming Arthur Chen and Chin-Tien Wang},
  journal={The Journal of general virology},
  year={2006},
  volume={87 Pt 7},
  pages={
          2041-6
        }
}
The proteolytic processing of human immunodeficiency virus (HIV) particles mediated by the viral pol-encoded protease (PR) is essential for viral infectivity. The pol coding sequence partially overlaps with the gag coding sequence and is translated as a Gag-Pol polyprotein precursor. Within Gag-Pol, the C-terminal p6(gag) domain is replaced by a transframe peptide referred to as p6*, which separates the Gag nucleocapsid domain from PR. Several previous in vitro studies have ascribed a PR… 
View on PubMed
doi.org
25 Citations
Highly Influential Citations
1
Background Citations
10
Methods Citations
1
Results Citations
3

Figures from this paper

25 Citations

Citation Type

Citation Type

Gag-Pol Transframe Domain p6* Is Essential for HIV-1 Protease-Mediated Virus Maturation
TLDR
The results suggest that p 6* is essential for triggering PR activation, p6* has a role in preventing premature virus processing, and the NC domain within Gag-Pol is not a major determinant of PR activation.
HIV-1 Mutant Assembly, Processing and Infectivity Expresses Pol Independent of Gag
TLDR
The data suggest that HIV-1 adopts a gag/pol ribosomal frameshifting mechanism to support virus assembly via the efficient modulation of Gag–Pol/Gag expression, as well as to promote viral enzyme packaging.
Uncoupling Human Immunodeficiency Virus Type 1 gag and pol Reading Frames: Role of the Transframe Protein p6* in Viral Replication
TLDR
To overcome limitations, a novel NL4-3-derived provirus was created by displacing the original frameshift signal to the 3′ end of the gag gene, thereby uncoupling the p6* gene sequence from the p1-p6gag reading frame and the resulting virus proved to be replication competent in different cell cultures and thus represents an elegant tool for detailed analysis of p 6* function.
Importance of Protease Cleavage Sites within and Flanking Human Immunodeficiency Virus Type 1 Transframe Protein p6* for Spatiotemporal Regulation of Protease Activation
TLDR
It is concluded that p6* cleavage is absolutely essential to allow complete activation of the PR and subsequent processing of the viral precursors.
Influence of extended mutations of the HIV-1 transframe protein p6 on Nef-dependent viral replication and infectivity in vitro.
Amino acid substitutions at the HIV-1 transframe region significantly impair virus infectivity
TLDR
The data strongly suggest that conserved Phe (F) residues at position 8 of p6* are involved in the PR maturation process, and this region within HIV-1 Gag-Pol plays a pivotal role in modulating PR activation.
Placement of Leucine Zipper Motifs at the Carboxyl Terminus of HIV-1 Protease Significantly Reduces Virion Production
TLDR
It is concluded that placement of a heterologous dimerization domain downstream of PR enhances PR-mediated Gag cleavage efficiency, implying that structural conformation, rather than the primary sequence outside of PR, is a major determinant of HIV-1 PR activation.
HIV-1 Nef Inhibits Protease Activity and Its Absence Alters Protein Content of Mature Viral Particles
TLDR
The hypothesis that the decreased infectivity typical of nef-deficient viruses is due to an abnormal function of the viral Protease, which is in turn associated with less mature particles being produced and the loss of Integrase content in these particles, is supported.
HIV-1 protease with leucine zipper fused at N-terminus exhibits enhanced linker amino acid-dependent activity
TLDR
The ability of HIV-1 C-terminal p6* amino acid residues to modulate PR activation contributes, at least in part, to their ability to counteract enhanced Gag cleavage induced by a leucine zipper substituted for a deleted p6*.
Formation of transient dimers by a retroviral protease.
Retroviral proteases have been shown previously to be only active as homodimers. They are essential to form the separate and active proteins from the viral precursors. Spumaretroviruses produce…
...
1
2
3
...

References

SHOWING 1-10 OF 47 REFERENCES
Contribution of the Gag-Pol transframe domain p6* and its coding sequence to morphogenesis and replication of human immunodeficiency virus type 1.
Competitive Inhibition of Human Immunodeficiency Virus Type-1 Protease by the Gag-Pol Transframe Protein*
TLDR
A role of the transframe protein p6* in regulating HIV-1 PR activity during viral replication is suggested, withKinetic analyses and cross-linking experiments revealed a competitive mechanism for PR inhibition by p6*.
Active human immunodeficiency virus protease is required for viral infectivity.
  • N. Kohl, E. Emini, +5 authors I. Sigal
  • Biology
    Proceedings of the National Academy of Sciences of the United States of America
  • 1988
TLDR
The results demonstrate that the HIV protease is an essential viral enzyme and, consequently, an attractive target for anti-HIV drugs.
Cleavage of Human Immunodeficiency Virus Type 1 Proteinase from the N-Terminally Adjacent p6* Protein Is Essential for Efficient Gag Polyprotein Processing and Viral Infectivity
TLDR
It is concluded that N-terminal release of PR from the HIV-1 polyprotein is essential for viral replication and it is suggested that extended versions of PR may have a transient function in the proteolytic cascade.
Characterization of human immunodeficiency virus type 1 Pr160 gag-pol mutants with truncations downstream of the protease domain.
Role of human immunodeficiency virus type 1-specific protease in core protein maturation and viral infectivity
TLDR
Results indicate that the HIV-1 protease plays a role not only in the maturation of the core proteins but also in the assembly of the virus and thus is required for viral infectivity.
Maintenance of the Gag/Gag-Pol Ratio Is Important for Human Immunodeficiency Virus Type 1 RNA Dimerization and Viral Infectivity
TLDR
These observations provide the first direct evidence that, in addition to proteolytic processing, the ratio of Gag/Gag-Pol proteins is also important for RNA dimerization and that stable RNA dimers are not required for encapsidation of genomic RNA in HIV-1.
Extensive regions of pol are required for efficient human immunodeficiency virus polyprotein processing and particle maturation.
TLDR
The severity of particle morphology abnormalities and of gag polyprotein processing impairment appeared to be affected both by the size and by the position of the deletions in pol, suggesting that the integrity of several pol domains within the gag-pol precursor is required for optimal protease activation and particle maturation.
Coding Sequences Upstream of the Human Immunodeficiency Virus Type 1 Reverse Transcriptase Domain in Gag-Pol Are Not Essential for Incorporation of the Pr160gag-pol into Virus Particles
TLDR
Test whether the HIV-1 Pol can be incorporated into virions on removal of the N-terminal Gag domain and to define sequences required for the incorporation of Gag-Pol into virion in more detail, a series of HIV GAG-Pol expression plasmids with various extensive deletions in the region upstream of the reverse transcriptase (RT) domain were constructed.
The virus-associated human immunodeficiency virus type 1 Gag-Pol carrying an active protease domain in the matrix region is severely defective both in autoprocessing and in trans processing of gag particles.
...
1
2
3
4
5
...