scholarly journals The HIV-1 Matrix Domain of Gag Is Required for Vpu Responsiveness during Particle Release

Virology ◽  
1997 ◽  
Vol 237 (1) ◽  
pp. 46-55 ◽  
Author(s):  
Yung-Hui Lee ◽  
Michael D. Schwartz ◽  
Antonito T. Panganiban
Keyword(s):  
Particle Release ◽  
Matrix Domain ◽  
Hiv 1

scholarly journals Activation of the Inositol (1,4,5)-Triphosphate Calcium Gate Receptor Is Required for HIV-1 Gag Release

2010 ◽  
Vol 84 (13) ◽  
pp. 6438-6451 ◽  
Author(s):  
Lorna S. Ehrlich ◽  
Gisselle N. Medina ◽  
Mahfuz B. Khan ◽  
Michael D. Powell ◽  
Katsuhiko Mikoshiba ◽  
...  
Keyword(s):  
Particle Production ◽  
Receptor Interaction ◽  
Particle Release ◽  
Virus Particles ◽  
Intracellular Ca ◽  
Necessary And Sufficient ◽  
Gag Assembly ◽  
Immature Virus ◽  
Interfering Rna ◽  
Hiv 1

ABSTRACT The structural precursor polyprotein, Gag, encoded by all retroviruses, including the human immunodeficiency virus type 1 (HIV-1), is necessary and sufficient for the assembly and release of particles that morphologically resemble immature virus particles. Previous studies have shown that the addition of Ca2+ to cells expressing Gag enhances virus particle production. However, no specific cellular factor has been implicated as mediator of Ca2+ provision. The inositol (1,4,5)-triphosphate receptor (IP3R) gates intracellular Ca2+ stores. Following activation by binding of its ligand, IP3, it releases Ca2+ from the stores. We demonstrate here that IP3R function is required for efficient release of HIV-1 virus particles. Depletion of IP3R by small interfering RNA, sequestration of its activating ligand by expression of a mutated fragment of IP3R that binds IP3 with very high affinity, or blocking formation of the ligand by inhibiting phospholipase C-mediated hydrolysis of the precursor, phosphatidylinositol-4,5-biphosphate, inhibited Gag particle release. These disruptions, as well as interference with ligand-receptor interaction using antibody targeted to the ligand-binding site on IP3R, blocked plasma membrane accumulation of Gag. These findings identify IP3R as a new determinant in HIV-1 trafficking during Gag assembly and introduce IP3R-regulated Ca2+ signaling as a potential novel cofactor in viral particle release.

The HIV-1 Vpu protein: a multifunctional enhancer of viral particle release

2003 ◽  
Vol 5 (11) ◽  
pp. 1029-1039 ◽  
Author(s):  
Stephan Bour ◽  
Klaus Strebel
Keyword(s):  
Viral Particle ◽  
Protein A ◽  
Particle Release ◽  
Hiv 1

scholarly journals HIV-1 Vpu's lipid raft association is dispensable for counteraction of the particle release restriction imposed by CD317/Tetherin

Virology ◽  
2012 ◽  
Vol 424 (1) ◽  
pp. 33-44 ◽  
Author(s):  
Joëlle V. Fritz ◽  
Nadine Tibroni ◽  
Oliver T. Keppler ◽  
Oliver T. Fackler
Keyword(s):  
Lipid Raft ◽  
Particle Release ◽  
Hiv 1

scholarly journals The RING-CH Ligase K5 Antagonizes Restriction of KSHV and HIV-1 Particle Release by Mediating Ubiquitin-Dependent Endosomal Degradation of Tetherin

2010 ◽  
Vol 6 (4) ◽  
pp. e1000843 ◽  
Author(s):  
Claire Pardieu ◽  
Raphaël Vigan ◽  
Sam J. Wilson ◽  
Alessandra Calvi ◽  
Trinity Zang ◽  
...  
Keyword(s):  
Particle Release ◽  
Hiv 1

scholarly journals Modulation of β-Catenin and E-Cadherin Interaction by Vpu Increases Human Immunodeficiency Virus Type 1 Particle Release

2008 ◽  
Vol 82 (8) ◽  
pp. 3932-3938 ◽  
Author(s):  
Aneeza Salim ◽  
Lee Ratner
Keyword(s):  
Human Immunodeficiency Virus ◽  
Human Immunodeficiency Virus Type ◽  
Virus Type ◽  
Particle Release ◽  
Viral Protein U ◽  
Immunodeficiency Virus ◽  
Infected Cells ◽  
Hiv 1 ◽  
E Cadherin

ABSTRACT Vpu (viral protein U) is a 17-kDa human immunodeficiency virus type 1 (HIV-1) accessory protein that enhances the release of particles from the surfaces of infected cells. Vpu recruits β-transducin repeat-containing protein (β-TrCP) and mediates proteasomal degradation of CD4. By sequestering β-TrCP away from other cellular substrates, Vpu leads to the stabilization of β-TrCP substrates such as β-catenin, IκBα, ATF4, and Cdc25A, but not of other substrates such as Emi1. This study shows that in addition to stabilizing β-catenin, Vpu leads to the depression of both total and β-catenin-associated E-cadherin levels through β-TrCP-dependent stabilization of the transcriptional repressor Snail. We showed that both downregulation of overall E-cadherin levels and dissociation of E-cadherin from β-catenin result in enhanced viral release. By contrast, the overexpression of E-cadherin or the prevention of the dissociation of E-cadherin from β-catenin results in depressed levels of virus release. Since E-cadherin is expressed only in dendritic cells and macrophages, and not in T cells, our data suggest that the HIV-1 vpu gene may have evolved to counteract different restrictions to assembly in different cells.

scholarly journals Virus Particle Release from Glycosphingolipid-Enriched Microdomains Is Essential for Dendritic Cell-Mediated Capture and Transfer of HIV-1 and Henipavirus

2014 ◽  
Vol 88 (16) ◽  
pp. 8813-8825 ◽  
Author(s):  
H. Akiyama ◽  
C. Miller ◽  
H. V. Patel ◽  
S. C. Hatch ◽  
J. Archer ◽  
...  
Keyword(s):  
Dendritic Cell ◽  
Virus Particle ◽  
Particle Release ◽  
Hiv 1

scholarly journals Generation and validation of a highly sensitive bioluminescent HIV-1 reporter vector that simplifies measurement of virus release

2020 ◽  
Author(s):  
James Kirui ◽  
Eric Freed
Keyword(s):  
Virus Particle ◽  
High Throughput Screening ◽  
Particle Production ◽  
Health Concern ◽  
Reporter Virus ◽  
Particle Assembly ◽  
Gag Protein ◽  
Minimal Impact ◽  
Particle Release ◽  
Hiv 1

Abstract Background The continued persistence of HIV-1 as a public health concern due to the lack of a cure calls for the development of new tools for studying replication of the virus. Here, we used NanoLuc, a small and extremely bright luciferase protein, to develop an HIV-1 bioluminescent reporter virus that simplifies functional measurement of virus particle production. Results The reporter virus encodes a Gag protein containing NanoLuc inserted between the matrix (MA) and capsid (CA) domains of Gag, thereby generating virus particles that package high levels of the NanoLuc reporter. We observe that inserting the NanoLuc protein within HIV-1 Gag has minimal impact on Gag expression and virus particle release. We show that the reporter virus recapitulates inhibition of HIV-1 particle release by Gag mutations, the restriction factor tetherin, and the small-molecule inhibitor amphotericin-B methyl ester. Conclusion These results demonstrate that this vector will provide a simple and rapid tool for functional studies of virus particle assembly and release and high-throughput screening for cellular factors and small-molecules that promote or inhibit HIV-1 particle production.

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