scholarly journals The HIV-1 envelope glycoprotein structure: nailing down a moving target

2017 ◽  
Vol 275 (1) ◽  
pp. 21-32 ◽  
Author(s):  
Andrew B Ward ◽  
Ian A Wilson
Keyword(s):  
Envelope Glycoprotein ◽  
Moving Target ◽  
Glycoprotein Structure ◽  
Hiv 1

scholarly journals HIV-1 envelope glycoprotein structure

2013 ◽  
Vol 23 (2) ◽  
pp. 268-276 ◽  
Author(s):  
Alan Merk ◽  
Sriram Subramaniam
Keyword(s):  
Envelope Glycoprotein ◽  
Glycoprotein Structure ◽  
Hiv 1

scholarly journals The convertases furin and PC1 can both cleave the human immunodeficiency virus (HIV)-1 envelope glycoprotein gp160 into gp120 (HIV-1 SU) and gp41 (HIV-I TM).

1994 ◽  
Vol 269 (16) ◽  
pp. 12240-12247 ◽  
Author(s):  
E. Decroly ◽  
M. Vandenbranden ◽  
J.M. Ruysschaert ◽  
J. Cogniaux ◽  
G.S. Jacob ◽  
...  
Keyword(s):  
Human Immunodeficiency Virus ◽  
Envelope Glycoprotein ◽  
Immunodeficiency Virus ◽  
Hiv 1

scholarly journals Cross-Reactive Antibodies With the Capacity to Mediate HIV-1 Envelope Glycoprotein–Targeted Antibody-Dependent Cellular Cytotoxicity Identified in HIV-2–Infected Individuals

2019 ◽  
Vol 219 (11) ◽  
pp. 1749-1754 ◽  
Author(s):  
Ingrid Karlsson ◽  
Jeanette Linnea Tingstedt ◽  
Gülşen Özkaya Şahin ◽  
Mikkel Hansen ◽  
Zsofia Szojka ◽  
...  
Keyword(s):  
Envelope Glycoprotein ◽  
Cellular Cytotoxicity ◽  
Antibody Dependent Cellular Cytotoxicity ◽  
Hiv 1

scholarly journals Targeting HIV-1 Envelope Glycoprotein Trimers to B Cells by Using APRIL Improves Antibody Responses

2011 ◽  
Vol 86 (5) ◽  
pp. 2488-2500 ◽  
Author(s):  
M. Melchers ◽  
I. Bontjer ◽  
T. Tong ◽  
N. P. Y. Chung ◽  
P. J. Klasse ◽  
...  
Keyword(s):  
B Cells ◽  
Envelope Glycoprotein ◽  
Antibody Responses ◽  
Hiv 1

scholarly journals Short Communication: Virion Aggregation by Neutralizing and Nonneutralizing Antibodies to the HIV-1 Envelope Glycoprotein

2015 ◽  
Vol 31 (11) ◽  
pp. 1160-1165 ◽  
Author(s):  
Marina R. Alexander ◽  
Rogier W. Sanders ◽  
John P. Moore ◽  
Per Johan Klasse
Keyword(s):  
Envelope Glycoprotein ◽  
Short Communication ◽  
Hiv 1

scholarly journals Antagonism to and Intracellular Sequestration of Human Tetherin by the Human Immunodeficiency Virus Type 2 Envelope Glycoprotein

2009 ◽  
Vol 83 (22) ◽  
pp. 11966-11978 ◽  
Author(s):  
Anna Le Tortorec ◽  
Stuart J. D. Neil
Keyword(s):  
Human Immunodeficiency Virus ◽  
Human Immunodeficiency Virus Type ◽  
Virus Type ◽  
Envelope Glycoprotein ◽  
Virus Assembly ◽  
Accessory Gene ◽  
Immunodeficiency Virus ◽  
T Cell Lines ◽  
Hiv 1 ◽  
Tetherin Antagonism

ABSTRACT Tetherin (CD317/BST-2), an interferon-induced membrane protein, restricts the release of nascent retroviral particles from infected cell surfaces. While human immunodeficiency virus type 1 (HIV-1) encodes the accessory gene vpu to overcome the action of tetherin, the lineage of primate lentiviruses that gave rise to HIV-2 does not. It has been previously reported that the HIV-2 envelope glycoprotein has a Vpu-like function in promoting virus release. Here we demonstrate that the HIV-2 Rod envelope glycoprotein (HIV-2 Rod Env) is a tetherin antagonist. Expression of HIV-2 Rod Env, but not that of HIV-1 or the closely related simian immunodeficiency virus (SIV) SIVmac1A11, counteracts tetherin-mediated restriction of Vpu-defective HIV-1 in a cell-type-specific manner. This correlates with the ability of the HIV-2 Rod Env to mediate cell surface downregulation of tetherin. Antagonism requires an endocytic motif conserved across HIV/SIV lineages in the gp41 cytoplasmic tail, but specificity for tetherin is governed by extracellular determinants in the mature Env protein. Coimmunoprecipitation studies suggest an interaction between HIV-2 Rod Env and tetherin, but unlike studies with Vpu, we found no evidence of tetherin degradation. In the presence of HIV-2 Rod Env, tetherin localization is restricted to the trans-Golgi network, suggesting Env-mediated effects on tetherin trafficking sequester it from virus assembly sites on the plasma membrane. Finally, we recapitulated these observations in HIV-2-infected CD4+ T-cell lines, demonstrating that tetherin antagonism and sequestration occur at physiological levels of Env expression during virus replication.

scholarly journals Expression-System-Dependent Modulation of HIV-1 Envelope Glycoprotein Antigenicity and Immunogenicity

2010 ◽  
Vol 403 (1) ◽  
pp. 131-147 ◽  
Author(s):  
Leopold Kong ◽  
Neil C. Sheppard ◽  
Guillaume B.E. Stewart-Jones ◽  
Cynthia L. Robson ◽  
Hongying Chen ◽  
...  
Keyword(s):  
Envelope Glycoprotein ◽  
Expression System ◽  
Hiv 1

scholarly journals Peptides presenting the binding site of human CD4 for the HIV-1 envelope glycoprotein gp120

2012 ◽  
Vol 8 ◽  
pp. 1858-1866 ◽  
Author(s):  
Julia Meier ◽  
Kristin Kassler ◽  
Heinrich Sticht ◽  
Jutta Eichler
Keyword(s):  
Amino Acids ◽  
Binding Site ◽  
Envelope Glycoprotein ◽  
Conformational Stability ◽  
Cellular Receptor ◽  
Binding Assays ◽  
Glycoprotein Gp120 ◽  
Dynamics Simulations ◽  
Key Residues ◽  
Hiv 1

Based on the structure of the HIV-1 glycoprotein gp120 in complex with its cellular receptor CD4, we have designed and synthesized peptides that mimic the binding site of CD4 for gp120. The ability of these peptides to bind to gp120 can be strongly enhanced by increasing their conformational stability through cyclization, as evidenced by binding assays, as well as through molecular-dynamics simulations of peptide–gp120 complexes. The specificity of the peptide–gp120 interaction was demonstrated by using peptide variants, in which key residues for the interaction with gp120 were replaced by alanine or D-amino acids.

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