scholarly journals Phosphorylation of Both Phosphoacceptor Sites in the HIV-1 Vpu Cytoplasmic Domain Is Essential for Vpu-Mediated ER Degradation of CD4

Virology ◽  
1997 ◽  
Vol 232 (1) ◽  
pp. 207-216 ◽  
Author(s):  
Mousumi Paul ◽  
M.Abdul Jabbar
Keyword(s):  
Cytoplasmic Domain ◽  
Hiv 1

scholarly journals Gag Regulates Association of Human Immunodeficiency Virus Type 1 Envelope with Detergent-Resistant Membranes

2006 ◽  
Vol 80 (11) ◽  
pp. 5292-5300 ◽  
Author(s):  
Jayanta Bhattacharya ◽  
Alexander Repik ◽  
Paul R. Clapham
Keyword(s):  
Human Immunodeficiency Virus ◽  
Lipid Rafts ◽  
Human Immunodeficiency Virus Type ◽  
Cytoplasmic Domain ◽  
Virus Particles ◽  
Immunodeficiency Virus ◽  
Detergent Resistant Membranes ◽  
Envelope Incorporation ◽  
Hiv 1

ABSTRACT Assembly of the human immunodeficiency virus type 1 (HIV-1) envelope glycoprotein on budding virus particles is important for efficient infection of target cells. In infected cells, lipid rafts have been proposed to form platforms for virus assembly and budding. Gag precursors partly associate with detergent-resistant membranes (DRMs) that are believed to represent lipid rafts. The cytoplasmic domain of the envelope gp41 usually carries palmitate groups that were also reported to confer DRM association. Gag precursors confer budding and carry envelope glycoproteins onto virions via specific Gag-envelope interactions. Thus, specific mutations in both the matrix domain of the Gag precursor and gp41 cytoplasmic domain abrogate envelope incorporation onto virions. Here, we show that HIV-1 envelope association with DRMs is directly influenced by its interaction with Gag. Thus, in the absence of Gag, envelope fails to associate with DRMs. A mutation in the p17 matrix (L30E) domain in Gag (Gag L30E) that abrogates envelope incorporation onto virions also eliminated envelope association with DRMs in 293T cells and in the T-cell line, MOLT 4. These observations are consistent with a requirement for an Env-Gag interaction for raft association and subsequent assembly onto virions. In addition to this observation, we found that mutations in the gp41 cytoplasmic domain that abrogated envelope incorporation onto virions and impaired infectivity of cell-free virus also eliminated envelope association with DRMs. On the basis of these observations, we propose that Gag-envelope interaction is essential for efficient envelope association with DRMs, which in turn is essential for envelope budding and assembly onto virus particles.

scholarly journals Identification of the Cellular Prohibitin 1/Prohibitin 2 Heterodimer as an Interaction Partner of the C-Terminal Cytoplasmic Domain of the HIV-1 Glycoprotein

2010 ◽  
Vol 84 (24) ◽  
pp. 13071-13071
Author(s):  
Vanessa Emerson ◽  
Denise Holtkotte ◽  
Tanya Pfeiffer ◽  
I-Hsuan Wang ◽  
Martina Schnölzer ◽  
...  
Keyword(s):  
Cytoplasmic Domain ◽  
Interaction Partner ◽  
Prohibitin 1 ◽  
Hiv 1

scholarly journals The Tale of the Long Tail: the Cytoplasmic Domain of HIV-1 gp41

2012 ◽  
Vol 87 (1) ◽  
pp. 2-15 ◽  
Author(s):  
T. S. Postler ◽  
R. C. Desrosiers
Keyword(s):  
Cytoplasmic Domain ◽  
Long Tail ◽  
Hiv 1

Structural consequences of phosphorylation of two serine residues in the cytoplasmic domain of HIV‐1 VpU

2008 ◽  
Vol 14 (7) ◽  
pp. 804-810 ◽  
Author(s):  
Marc Wittlich ◽  
Bernd W. Koenig ◽  
Dieter Willbold
Keyword(s):  
Cytoplasmic Domain ◽  
Hiv 1

scholarly journals Reassessment of the capacity of the HIV-1 Env cytoplasmic domain to trigger NF-κB activation

2018 ◽  
Vol 15 (1) ◽  
Author(s):  
Cyprien Beraud ◽  
Morgane Lemaire ◽  
Danielle Perez Bercoff
Keyword(s):  
Cytoplasmic Domain ◽  
Hiv 1

scholarly journals Replication of HIV-1 envelope protein cytoplasmic domain variants in permissive and restrictive cells

Virology ◽  
2019 ◽  
Vol 538 ◽  
pp. 1-10 ◽  
Author(s):  
August O. Staubus ◽  
Ayna Alfadhli ◽  
Robin Lid Barklis ◽  
Eric Barklis
Keyword(s):  
Envelope Protein ◽  
Cytoplasmic Domain ◽  
Hiv 1

scholarly journals Interaction between the Cytoplasmic Domain of ICAM-1 and Pr55Gag Leads to Acquisition of Host ICAM-1 by Human Immunodeficiency Virus Type 1

2004 ◽  
Vol 78 (21) ◽  
pp. 11916-11925 ◽  
Author(s):  
Yannick Beauséjour ◽  
Michel J. Tremblay
Keyword(s):  
Human Immunodeficiency Virus ◽  
Human Immunodeficiency Virus Type ◽  
Virus Type ◽  
Adhesion Molecule ◽  
Cytoplasmic Domain ◽  
Virus Infectivity ◽  
Immunodeficiency Virus ◽  
Selective Incorporation ◽  
Hiv 1

ABSTRACT We have examined the molecular basis for the selective incorporation of the adhesion molecule ICAM-1 within human immunodeficiency virus type 1 (HIV-1). The process of ICAM-1 incorporation was investigated by using different ICAM-1 constructs in combination with virus capture and immunoprecipitation studies, Western blot and confocal microscopy analyses, and infectivity assays. Experiments conducted with viruses bearing a truncated version of ICAM-1 revealed that the cytoplasmic domain of ICAM-1 governs insertion of this adhesion molecule into HIV-1. Further experiments suggested that there is an association between ICAM-1 and the virus-encoded Pr55Gag polyprotein. This study represents the first demonstration that structural Gag polyproteins play a key role in the uptake of a host-derived cell surface by the virus entity. Taken together, our results indicate that interactions between viral and cellular proteins are responsible for the selective uptake of host ICAM-1 by HIV-1. This observation describes a new strategy by which HIV-1 can modulate its replicative cycle, considering that insertion of ICAM-1 within nascent virions has been shown to increase virus infectivity.

scholarly journals “Cytoplasmic domain effects on exposure of co-receptor-binding sites of HIV-1 Env”

2016 ◽  
Vol 161 (11) ◽  
pp. 3011-3018 ◽  
Author(s):  
Andrei N. Vzorov ◽  
Richard W. Compans
Keyword(s):  
Receptor Binding ◽  
Binding Sites ◽  
Cytoplasmic Domain ◽  
Hiv 1

scholarly journals Membrane interactions and alignment of structures within the HIV-1 Vpu cytoplasmic domain: effect of phosphorylation of serines 52 and 56

FEBS Letters ◽  
2000 ◽  
Vol 482 (3) ◽  
pp. 220-224 ◽  
Author(s):  
Peter Henklein ◽  
Rudolf Kinder ◽  
Ulrich Schubert ◽  
Burkhard Bechinger
Keyword(s):  
Cytoplasmic Domain ◽  
Membrane Interactions ◽  
Hiv 1
Sign in / Sign up

Export Citation Format

Share Document