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Results: 1 to 3 of 3

Publication Record


Maturation of the viral core enhances the fusion of HIV-1 particles with primary human T cells and monocyte-derived macrophages.
Jiang J, Aiken C
(2006) Virology 346: 460-8
MeSH Terms: CD4-Positive T-Lymphocytes, Cell Line, HIV Envelope Protein gp41, HIV-1, Humans, Macrophages, Membrane Fusion, Receptors, CCR5, Receptors, CXCR4, Receptors, HIV, Virus Replication
Show Abstract · Added February 19, 2015
HIV-1 infection requires fusion of viral and cellular membranes in a reaction catalyzed by the viral envelope proteins gp120 and gp41. We recently reported that efficient HIV-1 particle fusion with target cells is linked to maturation of the viral core by an activity of the gp41 cytoplasmic domain. Here, we show that maturation enhances the fusion of a variety of recombinant viruses bearing primary and laboratory-adapted Env proteins with primary human CD4+ T cells. Overall, HIV-1 fusion was more dependent on maturation for viruses bearing X4-tropic envelope proteins than for R5-tropic viruses. Fusion of HIV-1 with monocyte-derived macrophages was also dependent on particle maturation. We conclude that the ability to couple fusion to particle maturation is a common feature of HIV-1 Env proteins and may play an important role during HIV-1 replication in vivo.
0 Communities
1 Members
0 Resources
11 MeSH Terms
Human immunodeficiency virus type 1 particles pseudotyped with envelope proteins that fuse at low pH no longer require Nef for optimal infectivity.
Chazal N, Singer G, Aiken C, Hammarskjöld ML, Rekosh D
(2001) J Virol 75: 4014-8
MeSH Terms: Animals, Anti-Bacterial Agents, Antibodies, Viral, Cell Line, Gene Deletion, Gene Products, nef, HIV Envelope Protein gp120, HIV-1, HeLa Cells, Humans, Hydrogen-Ion Concentration, Immune Sera, Macrolides, Membrane Fusion, Membrane Glycoproteins, Molecular Sequence Data, Neutralization Tests, Receptors, HIV, Viral Envelope Proteins, nef Gene Products, Human Immunodeficiency Virus
Show Abstract · Added February 19, 2015
We have investigated the effects of Nef on infectivity in the context of various viral envelope proteins. These experiments were performed with a minimal vector system where Nef is the only accessory protein present. Our results support the hypothesis that the route of entry influences the ability of Nef to enhance human immunodeficiency virus (HIV) infectivity. We show that HIV particles pseudotyped with Ebola virus glycoprotein or vesicular stomatitis virus glycoprotein (VSV-G), which fuse at low pH, do not require Nef for optimal infectivity. In contrast, Nef significantly enhances the infectivity of virus particles that contain envelope proteins that fuse at neutral pH (CCR5-dependent HIV Env, CXCR4-dependent HIV Env, or amphotropic murine leukemia virus Env). In addition, our results demonstrate that virus particles containing mixed CXCR4-dependent HIV and VSV-G envelope proteins show a conditional requirement for Nef for optimal infectivity, depending on which protein is allowed to facilitate entry.
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1 Members
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20 MeSH Terms
Analysis of fractalkine receptor CX(3)CR1 function by targeted deletion and green fluorescent protein reporter gene insertion.
Jung S, Aliberti J, Graemmel P, Sunshine MJ, Kreutzberg GW, Sher A, Littman DR
(2000) Mol Cell Biol 20: 4106-14
MeSH Terms: Animals, CX3C Chemokine Receptor 1, Gene Expression, Gene Targeting, Genes, Reporter, Green Fluorescent Proteins, Luminescent Proteins, Mice, Mice, Mutant Strains, Mutagenesis, Insertional, Phenotype, Receptors, Cytokine, Receptors, HIV
Show Abstract · Added August 11, 2015
The seven-transmembrane receptor CX(3)CR1 is a specific receptor for the novel CX(3)C chemokine fractalkine (FKN) (neurotactin). In vitro data suggest that membrane anchoring of FKN, and the existence of a shed, soluble FKN isoform allow for both adhesive and chemoattractive properties. Expression on activated endothelium and neurons defines FKN as a potential target for therapeutic intervention in inflammatory conditions, particularly central nervous system diseases. To investigate the physiological function of CX(3)CR1-FKN interactions, we generated a mouse strain in which the CX(3)CR1 gene was replaced by a green fluorescent protein (GFP) reporter gene. In addition to the creation of a mutant CX(3)CR1 locus, this approach enabled us to assign murine CX(3)CR1 expression to monocytes, subsets of NK and dendritic cells, and the brain microglia. Analysis of CX(3)CR1-deficient mice indicates that CX(3)CR1 is the only murine FKN receptor. Yet, defying anticipated FKN functions, absence of CX(3)CR1 interferes neither with monocyte extravasation in a peritonitis model nor with DC migration and differentiation in response to microbial antigens or contact sensitizers. Furthermore, a prominent response of CX(3)CR1-deficient microglia to peripheral nerve injury indicates unimpaired neuronal-glial cross talk in the absence of CX(3)CR1.
0 Communities
0 Members
1 Resources
13 MeSH Terms