Relevant bibliographies by topics / SIV Envelope Glycoprotein

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  1. Journal articles
  2. Dissertations / Theses

Academic literature on the topic 'SIV Envelope Glycoprotein'

Author: Grafiati
Published: 4 June 2021
Last updated: 16 February 2022

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Journal articles on the topic "SIV Envelope Glycoprotein"

1

Chen, Bing, Yifan Cheng, Lesley Calder, et al. "A Chimeric Protein of Simian Immunodeficiency Virus Envelope Glycoprotein gp140 and Escherichia coli Aspartate Transcarbamoylase." Journal of Virology 78, no. 9 (2004): 4508–16. http://dx.doi.org/10.1128/jvi.78.9.4508-4516.2004.

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ABSTRACT The envelope glycoproteins of the human immunodeficiency virus and the related simian immunodeficiency virus (SIV) mediate viral entry into host cells by fusing viral and target cell membranes. We have reported expression, purification, and characterization of gp140 (also called gp160e), the soluble, trimeric ectodomain of the SIV envelope glycoprotein, gp160 (B. Chen et al., J. Biol. Chem. 275:34946-34953, 2000). We have now expressed and purified chimeric proteins of SIV gp140 and its variants with the catalytic subunit (C) of Escherichia coli aspartate transcarbamoylase (ATCase). T
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Schenten, Dominik, Luisa Marcon, Gunilla B. Karlsson, et al. "Effects of Soluble CD4 on Simian Immunodeficiency Virus Infection of CD4-Positive and CD4-Negative Cells." Journal of Virology 73, no. 7 (1999): 5373–80. http://dx.doi.org/10.1128/jvi.73.7.5373-5380.1999.

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ABSTRACT A soluble form of the CD4 receptor (sCD4) can either enhance or inhibit the infection of cells by simian immunodeficiency virus (SIV) and human immunodeficiency virus. We investigated the basis for these varying effects by studying the entry of three SIV isolates into CD4-positive and CD4-negative cells expressing different chemokine receptors. Infection of CD4-negative cells depended upon the viral envelope glycoproteins and upon the chemokine receptor, with CCR5 and gpr15 being more efficient than STRL33. Likewise, enhancement of infection by sCD4 was observed when CCR5- and gpr15-e
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Sauter, M. M., A. Pelchen-Matthews, R. Bron, et al. "An internalization signal in the simian immunodeficiency virus transmembrane protein cytoplasmic domain modulates expression of envelope glycoproteins on the cell surface." Journal of Cell Biology 132, no. 5 (1996): 795–811. http://dx.doi.org/10.1083/jcb.132.5.795.

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A Tyr to Cys mutation at amino acid position 723 in the cytoplasmic domain of the simian immunodeficiency virus (SIV) transmembrane (TM) molecule has been shown to increase expression of envelope glycoproteins on the surface of infected cells. Here we show that Tyr-723 contributes to a sorting signal that directs the rapid endocytosis of viral glycoproteins from the plasma membrane via coated pits. On cells infected by SIVs with a Tyr at position 723, envelope glycoproteins were transiently expressed on the cell surface and then rapidly endocytosed. Similar findings were noted for envelope mol
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Evans, David T., Karl C. Tillman, and Ronald C. Desrosiers. "Envelope Glycoprotein Cytoplasmic Domains from Diverse Lentiviruses Interact with the Prenylated Rab Acceptor." Journal of Virology 76, no. 1 (2002): 327–37. http://dx.doi.org/10.1128/jvi.76.1.327-337.2002.

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ABSTRACT Lentivirus envelope glycoproteins have unusually long cytoplasmic domains compared to those of other retroviruses. To identify cellular binding partners of the simian immunodeficiency virus (SIV) envelope transmembrane protein (gp41) cytoplasmic domain (CD), we performed a yeast two-hybrid screen of a phytohemagglutinin-activated human T-cell cDNA library with the SIV gp41 CD. The majority of positive clones (50 of 54) encoded the prenylated Rab acceptor (PRA1). PRA1 is a 21-kDa protein associated with Golgi membranes that binds to prenylated Rab proteins in their GTP-bound state. Whi
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Vzorov, A. N., and R. W. Compans. "Effect of the Cytoplasmic Domain of the Simian Immunodeficiency Virus Envelope Protein on Incorporation of Heterologous Envelope Proteins and Sensitivity to Neutralization." Journal of Virology 74, no. 18 (2000): 8219–25. http://dx.doi.org/10.1128/jvi.74.18.8219-8225.2000.

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ABSTRACT In addition to the viral envelope (Env) proteins, host cell-derived proteins have been reported to be present in human immunodeficiency virus and simian immunodeficiency virus (SIV) envelopes, and it has been postulated that they may play a role in infection. We investigated whether the incorporation of host cell proteins is affected by the structure and level of incorporation of viral Env proteins. To compare the cellular components incorporated into SIV particles and how this is influenced by the structure of the cytoplasmic domain, we compared SIV virions with full-length and trunc
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Hart, T. K., A. M. Klinkner, J. Ventre, and P. J. Bugelski. "Morphometric analysis of envelope glycoprotein gp120 distribution on HIV-1 virions." Journal of Histochemistry & Cytochemistry 41, no. 2 (1993): 265–71. http://dx.doi.org/10.1177/41.2.7678271.

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The surface of HIV-1, like that of other retroviruses, is studied with virally encoded glycoproteins which appear ultrastructurally as electron-dense spikes or knobs. The glycoprotein that forms the spike structure, gp120, is non-covalently bound to the transmembrane glycoprotein gp41. Mature HIV-1 virions do not have as many spikes as the genetically related retroviruses HIV-2 and SIV. gp120 is lost from HIV-1 during viral morphogenesis and after incubation of the virus with the soluble form of cellular receptor CD4. In this study we used ultrastructural cytochemistry and morphometry to quant
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Chertova, Elena, Julian W. Bess,, Bruce J. Crise, et al. "Envelope Glycoprotein Incorporation, Not Shedding of Surface Envelope Glycoprotein (gp120/SU), Is the Primary Determinant of SU Content of Purified Human Immunodeficiency Virus Type 1 and Simian Immunodeficiency Virus." Journal of Virology 76, no. 11 (2002): 5315–25. http://dx.doi.org/10.1128/jvi.76.11.5315-5325.2002.

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ABSTRACT Human immunodeficiency virus type 1 (HIV-1) and simian immunodeficiency virus (SIV) particles typically contain small amounts of the surface envelope protein (SU), and this is widely believed to be due to shedding of SU from mature virions. We purified proteins from HIV-1 and SIV isolates using procedures which allow quantitative measurements of viral protein content and determination of the ratios of gag- and env-encoded proteins in virions. All of the HIV-1 and most of the SIV isolates examined contained low levels of envelope proteins, with Gag:Env ratios of approximately 60:1. Bas
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8

Hu, S., K. Abrams, G. Barber, et al. "Protection of macaques against SIV infection by subunit vaccines of SIV envelope glycoprotein gp160." Science 255, no. 5043 (1992): 456–59. http://dx.doi.org/10.1126/science.1531159.

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9

Berlioz-Torrent, Clarisse, Barbara L. Shacklett, Lars Erdtmann, et al. "Interactions of the Cytoplasmic Domains of Human and Simian Retroviral Transmembrane Proteins with Components of the Clathrin Adaptor Complexes Modulate Intracellular and Cell Surface Expression of Envelope Glycoproteins." Journal of Virology 73, no. 2 (1999): 1350–61. http://dx.doi.org/10.1128/jvi.73.2.1350-1361.1999.

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ABSTRACT The cytoplasmic domains of the transmembrane (TM) envelope proteins (TM-CDs) of most retroviruses have a Tyr-based motif, YXXØ, in their membrane-proximal regions. This signal is involved in the trafficking and endocytosis of membrane receptors via clathrin-associated AP-1 and AP-2 adaptor complexes. We have used CD8-TM-CD chimeras to investigate the role of the Tyr-based motif of human immunodeficiency virus type 1 (HIV-1), simian immunodeficiency virus (SIV), and human T-leukemia virus type 1 (HTLV-1) TM-CDs in the cell surface expression of the envelope glycoprotein. Flow cytometry
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Manrique, Julieta M., Cristina C. P. Celma, Eric Hunter, José L. Affranchino, and Silvia A. González. "Positive and Negative Modulation of Virus Infectivity and Envelope Glycoprotein Incorporation into Virions by Amino Acid Substitutions at the N Terminus of the Simian Immunodeficiency Virus Matrix Protein." Journal of Virology 77, no. 20 (2003): 10881–88. http://dx.doi.org/10.1128/jvi.77.20.10881-10888.2003.

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ABSTRACT The matrix (MA) protein of the simian immunodeficiency viruses (SIVs) is encoded by the amino-terminal region of the Gag precursor and is the component of the viral capsid that lines the inner surface of the virus envelope. Previously, we identified domains in the SIV MA that are involved in the transport of Gag to the plasma membrane and in particle assembly. In this study, we characterized the role in the SIV life cycle of highly conserved residues within the SIV MA region spanning the two N-terminal α-helices H1 and H2. Our analyses identified two classes of MA mutants: (i) viruses
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Dissertations / Theses on the topic "SIV Envelope Glycoprotein"

1

Bowers, Katherine Elisabeth. "Sorting of CD4 and the SIV envelope glycoprotein in the endocytic pathway." Thesis, University College London (University of London), 1998. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.286733.

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Postler, Thomas Verfasser], and Bernhard [Akademischer Betreuer] [Fleckenstein. "The Cytoplasmic Domain of the HIV-1 and SIV Envelope Glycoprotein: Functional Properties and Topology / Thomas Postler. Betreuer: Bernhard Fleckenstein." Erlangen : Universitätsbibliothek der Universität Erlangen-Nürnberg, 2012. http://d-nb.info/1024198774/34.

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Yen, Po-Jen. "SIV envelope glycoprotein determinants of macrophage tropism and their relationship to neutralization sensitivity and CD4-independent cell-to-cell transmission." Thesis, Harvard University, 2013. http://dissertations.umi.com/gsas.harvard:11188.

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Macrophages are target cells for human immunodeficiency virus (HIV) and simian immunodeficiency virus (SIV) infection that serve as viral reservoirs in brain, lung, gut, and other tissues, and play important roles in disease pathogenesis, particularly HIV/SIV-associated neurological disease. Macrophages express low levels of the HIV/SIV receptor CD4, but mechanisms by which macrophage-tropic viruses use low CD4 to mediate spreading infections are poorly understood. One mechanism involves enhanced envelope glycoprotein (Env) interaction with CD4 or CCR5, but this phenotype is frequently associa
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Howard, Megan Wilder. "Coronavirus mediated membrane fusion /." Connect to full text via ProQuest. Limited to UCD Anschutz Medical Campus, 2008. http://proquest.umi.com/pqdweb?did=1552538711&sid=1&Fmt=6&clientId=18952&RQT=309&VName=PQD.

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Thesis (Ph.D. in Microbiology) -- University of Colorado Denver, 2008.<br>Typescript. Includes bibliographical references (leaves 161-183). Free to UCD Anschutz Medical Campus. Online version available via ProQuest Digital Dissertations;
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Fulcher, Jennifer Ann. "Novel galectin-1 functions at the host-pathogen interface interactions with Nipah virus envelope glycoproteins and multifunctional roles in dendritic cell activation and development /." Diss., Restricted to subscribing institutions, 2008. http://proquest.umi.com/pqdweb?did=1680017811&sid=14&Fmt=2&clientId=1564&RQT=309&VName=PQD.

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