Other search tools

About this data

The publication data currently available has been vetted by Vanderbilt faculty, staff, administrators and trainees. The data itself is retrieved directly from NCBI's PubMed and is automatically updated on a weekly basis to ensure accuracy and completeness.

If you have any questions or comments, please contact us.

Results: 11 to 17 of 17

Publication Record

Connections

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
The type 1 angiotensin II receptor tail affects receptor targeting, internalization, and membrane fusion properties.
Becker BN, Cheng HF, Hammond TG, Harris RC
(2004) Mol Pharmacol 65: 362-9
MeSH Terms: Amino Acid Sequence, Angiotensin II, Animals, Endocytosis, LLC-PK1 Cells, Membrane Fusion, Molecular Sequence Data, Peptide Fragments, Protein Binding, Rabbits, Rats, Receptor, Angiotensin, Type 1, Swine
Show Abstract · Added January 28, 2014
Endocytosis modulates cell responses by removing and recycling receptors from the cell surface. Type I angiotensin II receptors (AT1R) are somewhat unique in that they are expressed at apical (AP) and basolateral (BL) membranes in proximal tubule cells and both receptor sites undergo endocytosis. We analyzed AT1R cytoplasmic (-COOH) tail deletion mutants to determine whether classic AT1R endocytosis motifs functioned similarly in polarized cells and simultaneously altered receptor properties. Serially truncating the AT1R tail had little effect on AP/BL AT1R distribution as determined by 125I-angiotensin II binding in LLCPK(Cl4) cells transfected with an AT1R transcript. AP AT1R expression required the proximal 12 amino acids in the AT1R-COOH tail. Deleting all but the proximal 12 aa of the AT1R-COOH tail (T316L mutant) decreased AP AT1R internalization at 20 min (17 +/- 6%; p < 0.05 versus full-length; n = 5) and inhibited AP AT1R-stimulated arachidonic acid release (counts released per milligram of protein at 20 min: full-length, 18,762 +/- 4018; T316L, 2430 +/- 1711; n = 4; p < 0.02). Endosomal fusion assays were performed using peptide sequences of regions in the AT1R tail involved in endocytosis (YFLQLLKYIPP [LL] and LSTKMSTLSY [STL]). Peptide STL significantly inhibited endosomal fusion (22 +/- 10% of control; n = 5; p < 0.05 versus positive control). Peptide LL had no significant inhibitory effect. AT(1)R in polarized cells contain dominant endocytosis signals but these motifs do not correlate with AP or BL AT1R expression. Moreover, peptide sequences within the AT1R-COOH tail necessary for endocytosis also modulate endosomal fusion properties.
1 Communities
1 Members
0 Resources
13 MeSH Terms
Nef does not affect the efficiency of human immunodeficiency virus type 1 fusion with target cells.
Tobiume M, Lineberger JE, Lundquist CA, Miller MD, Aiken C
(2003) J Virol 77: 10645-50
MeSH Terms: CD4 Antigens, Gene Products, nef, HIV-1, HeLa Cells, Humans, Membrane Fusion, Virion, nef Gene Products, Human Immunodeficiency Virus
Show Abstract · Added February 19, 2015
The human immunodeficiency virus type 1 (HIV-1) accessory protein Nef stimulates viral infectivity by an unknown mechanism. Recent studies have suggested that Nef may act by regulating the efficiency of virus entry into cells. Here we provide evidence to the contrary. Using a quantitative assay of HIV-1 virus-cell fusion, we observed equivalent rates and extents of fusion of wild-type and Nef-defective HIV-1 particles with MT-4 cells and CD4-expressing HeLa cells. In studies using soluble CD4 (sCD4) to inhibit infection, wild-type and Nef-defective HIV-1 escaped the sCD4 block with similar kinetics. We conclude that Nef acts at a postentry step in infection, probably by facilitating intracellular transport of the HIV-1 ribonucleoprotein complex.
0 Communities
1 Members
0 Resources
8 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.
0 Communities
1 Members
0 Resources
20 MeSH Terms
Utilization of sialic acid as a coreceptor enhances reovirus attachment by multistep adhesion strengthening.
Barton ES, Connolly JL, Forrest JC, Chappell JD, Dermody TS
(2001) J Biol Chem 276: 2200-11
MeSH Terms: Animals, Biosensing Techniques, Cell Line, Humans, Kinetics, Membrane Fusion, Mice, N-Acetylneuraminic Acid, Protein Binding, Receptors, Virus, Reoviridae, Surface Plasmon Resonance
Show Abstract · Added December 10, 2013
Many serotype 3 reoviruses bind to two different host cell molecules, sialic acid and an unidentified protein, using discrete receptor-binding domains in viral attachment protein, final sigma1. To determine mechanisms by which these receptor-binding events cooperate to mediate cell attachment, we generated isogenic reovirus strains that differ in the capacity to bind sialic acid. Strain SA+, but not SA-, bound specifically to sialic acid on a biosensor chip with nanomolar avidity. SA+ displayed 5-fold higher avidity for HeLa cells when compared with SA-, although both strains recognized the same proteinaceous receptor. Increased avidity of SA+ binding was mediated by increased k(on). Neuraminidase treatment to remove cell-surface sialic acid decreased the k(on) of SA+ to that of SA-. Increased k(on) of SA+ enhanced an infectious attachment process, since SA+ was 50-100-fold more efficient than SA- at infecting HeLa cells in a kinetic fluorescent focus assay. Sialic acid binding was operant early during SA+ attachment, since the capacity of soluble sialyllactose to inhibit infection decreased rapidly during the first 20 min of adsorption. These results indicate that reovirus binding to sialic acid enhances virus infection through adhesion of virus to the cell surface where access to a proteinaceous receptor is thermodynamically favored.
0 Communities
1 Members
0 Resources
12 MeSH Terms
In vivo dynamics of nuclear pore complexes in yeast.
Bucci M, Wente SR
(1997) J Cell Biol 136: 1185-99
MeSH Terms: Biological Transport, Fungal Proteins, Green Fluorescent Proteins, Luminescent Proteins, Macromolecular Substances, Membrane Fusion, Movement, Nuclear Envelope, Nuclear Proteins, Recombinant Fusion Proteins, Reproduction, Saccharomyces cerevisiae
Show Abstract · Added March 21, 2014
While much is known about the role of nuclear pore complexes (NPCs) in nucleocytoplasmic transport, the mechanism of NPC assembly into pores formed through the double lipid bilayer of the nuclear envelope is not well defined. To investigate the dynamics of NPCs, we developed a live-cell assay in the yeast Saccharomyces cerevisiae. The nucleoporin Nup49p was fused to the green fluorescent protein (GFP) of Aequorea victoria and expressed in nup49 null haploid yeast cells. When the GFP-Nup49p donor cell was mated with a recipient cell harboring only unlabeled Nup49p, the nuclei fused as a consequence of the normal mating process. By monitoring the distribution of the GFP-Nup49p, we could assess whether NPCs were able to move from the donor section of the nuclear envelope to that of the recipient nucleus. We observed that fluorescent NPCs moved and encircled the entire nucleus within 25 min after fusion. When assays were done in mutant kar1-1 strains, where nuclear fusion does not occur, GFP-Nup49p appearance in the recipient nucleus occurred at a very slow rate, presumably due to new NPC biogenesis or to exchange of GFP-Nup49p into existing recipient NPCs. Interestingly, in a number of existing mutant strains, NPCs are clustered together at permissive growth temperatures. This has been explained with two different hypotheses: by movement of NPCs through the double nuclear membranes with subsequent clustering at a central location; or, alternatively, by assembly of all NPCs at a central location (such as the spindle pole body) with NPCs in mutant cells unable to move away from this point. Using the GFP-Nup49p system with a mutant in the NPC-associated factor Gle2p that exhibits formation of NPC clusters only at 37 degrees C, it was possible to distinguish between these two models for NPC dynamics. GFP-Nup49p-labeled NPCs, assembled at 23 degrees C, moved into clusters when the cells were shifted to growth at 37 degrees C. These results indicate that NPCs can move through the double nuclear membranes and, moreover, can do so to form NPC clusters in mutant strains. Such clusters may result by releasing NPCs from a nuclear tether, or by disappearance of a protein that normally prevents pore aggregation. This system represents a novel approach for identifying regulators of NPC assembly and movement in the future.
0 Communities
1 Members
0 Resources
12 MeSH Terms
Infectious subvirion particles of reovirus type 3 Dearing exhibit a loss in infectivity and contain a cleaved sigma 1 protein.
Nibert ML, Chappell JD, Dermody TS
(1995) J Virol 69: 5057-67
MeSH Terms: Animals, Antibodies, Monoclonal, Capsid Proteins, Chymotrypsin, Hemagglutinins, Viral, Hydrolysis, L Cells, Mammalian orthoreovirus 3, Membrane Fusion, Mice, Neuraminidase, Trypsin, Viral Proteins, Virion, Virulence
Show Abstract · Added December 10, 2013
Mammalian reoviruses exhibit differences in the capacity to grow in intestinal tissue: reovirus type 1 Lang (T1L), but not type 3 Dearing (T3D), can be recovered in high titer from intestinal tissue of newborn mice after oral inoculation. We investigated whether in vitro protease treatment of virions of T1L and T3D, using conditions to generate infectious subvirion particles (ISVPs) as occurs in the intestinal lumen of mice (D. K. Bodkin, M. L. Nibert, and B. N. Fields, J. Virol. 63:4676-4681, 1989), affects viral infectivity. Chymotrypsin treatment of T1L was associated with a 2-fold increase in viral infectivity, whereas identical treatment of T3D resulted in a 10-fold decrease in infectivity. Using sodium dodecyl sulfate-polyacrylamide gel electrophoresis, we found that loss of T3D infectivity was correlated with cleavage of its sigma 1 protein. We used reassortant viruses to identify viral determinants of infectivity loss and sigma 1 cleavage and found that both phenotypes segregate with the sigma 1-encoding S1 gene. Comparable results were obtained when trypsin treatment of virions of T1L and T3D was used. In experiments to determine the fate of sigma 1 fragments following cleavage, the capacity of anti-sigma 1 monoclonal antibody G5 to neutralize infectivity of T3D ISVPs was significantly decreased in comparison with its capacity to neutralize infectivity of virions, suggesting that a sigma 1 domain bound by G5 is lost from viral particles after proteolytic digestion. In contrast to the decrease in infectivity, chymotrypsin treatment of T3D virions leading to generation of ISVPs resulted in a 10-fold increase in their capacity to produce hemagglutination, indicating that a domain of sigma 1 important for binding to sialic acid remains associated with viral particles after sigma 1 cleavage. Neuraminidase treatment of L cells substantially decreased the yield of T3D ISVPs in comparison with the yield of virions, indicating that a sigma 1 domain important for binding sialic acid also can mediate attachment of T3D ISVPs to L cells and lead to productive infection. These results suggest that cleavage of T3D sigma 1 protein following oral inoculation of newborn mice is at least partly responsible for the decreased growth of T3D in the intestine and provide additional evidence that T3D sigma 1 contains more than a single receptor-binding domain.
0 Communities
1 Members
0 Resources
15 MeSH Terms