HIV-1 Variants with Reduced Sensitivity to Sulfated Oligosaccharide Muparfostat Contain Mutations in the Envelope Glycoproteins gp120 and gp41

2013 ◽  
Vol 05 (03) ◽  
Author(s):  
Joanna Said
Keyword(s):  
Envelope Glycoproteins ◽  
Sulfated Oligosaccharide ◽  
Hiv 1

Role of HIV-1 Envelope Glycoproteins Conformation and Accessory Proteins on ADCC Responses

2015 ◽  
Vol 14 (1) ◽  
pp. 9-23 ◽  
Author(s):  
Maxime Veillette ◽  
Jonathan Richard ◽  
Marzena Pazgier ◽  
George K. Lewis ◽  
Matthew S. Parsons ◽  
...  
Keyword(s):  
Envelope Glycoproteins ◽  
Accessory Proteins ◽  
Hiv 1

scholarly journals Human Plasmacytoid Dendritic Cells Efficiently Capture HIV-1 Envelope Glycoproteins via CD4 for Antigen Presentation

2013 ◽  
Vol 191 (1) ◽  
pp. 60-69 ◽  
Author(s):  
Kerrie J. Sandgren ◽  
Anna Smed-Sörensen ◽  
Mattias N. Forsell ◽  
Martina Soldemo ◽  
William C. Adams ◽  
...  
Keyword(s):  
Dendritic Cells ◽  
Antigen Presentation ◽  
Plasmacytoid Dendritic Cells ◽  
Envelope Glycoproteins ◽  
Hiv 1

scholarly journals HIV-1 tropism for the central nervous system: Brain-derived envelope glycoproteins with lower CD4 dependence and reduced sensitivity to a fusion inhibitor

Virology ◽  
2006 ◽  
Vol 346 (1) ◽  
pp. 169-179 ◽  
Author(s):  
Julio Martín-García ◽  
Wei Cao ◽  
Angel Varela-Rohena ◽  
Matthew L. Plassmeyer ◽  
Francisco González-Scarano
Keyword(s):  
Central Nervous System ◽  
Nervous System ◽  
Envelope Glycoproteins ◽  
Fusion Inhibitor ◽  
The Central Nervous System ◽  
Hiv 1

scholarly journals N-linked glycosylation in the CXCR4 N-terminus inhibits binding to HIV-1 envelope glycoproteins

Virology ◽  
2004 ◽  
Vol 324 (1) ◽  
pp. 140-150 ◽  
Author(s):  
Jianbin Wang ◽  
Gregory J Babcock ◽  
Hyeryun Choe ◽  
Michael Farzan ◽  
Joseph Sodroski ◽  
...  
Keyword(s):  
Envelope Glycoproteins ◽  
N Terminus ◽  
Hiv 1

scholarly journals A V3 Loop-Dependent gp120 Element Disrupted by CD4 Binding Stabilizes the Human Immunodeficiency Virus Envelope Glycoprotein Trimer

2010 ◽  
Vol 84 (7) ◽  
pp. 3147-3161 ◽  
Author(s):  
Shi-Hua Xiang ◽  
Andrés Finzi ◽  
Beatriz Pacheco ◽  
Kevin Alexander ◽  
Wen Yuan ◽  
...  
Keyword(s):  
Human Immunodeficiency Virus ◽  
Receptor Binding ◽  
Chemokine Receptor ◽  
Chemokine Receptors ◽  
Envelope Glycoproteins ◽  
V3 Loop ◽  
Virus Envelope ◽  
Hydrophobic Patch ◽  
Immunodeficiency Virus ◽  
Hiv 1

ABSTRACT Human immunodeficiency virus (HIV-1) entry into cells is mediated by a trimeric complex consisting of noncovalently associated gp120 (exterior) and gp41 (transmembrane) envelope glycoproteins. The binding of gp120 to receptors on the target cell alters the gp120-gp41 relationship and activates the membrane-fusing capacity of gp41. Interaction of gp120 with the primary receptor, CD4, results in the exposure of the gp120 third variable (V3) loop, which contributes to binding the CCR5 or CXCR4 chemokine receptors. We show here that insertions in the V3 stem or polar substitutions in a conserved hydrophobic patch near the V3 tip result in decreased gp120-gp41 association (in the unliganded state) and decreased chemokine receptor binding (in the CD4-bound state). Subunit association and syncytium-forming ability of the envelope glycoproteins from primary HIV-1 isolates were disrupted more by V3 changes than those of laboratory-adapted HIV-1 envelope glycoproteins. Changes in the gp120 β2, β19, β20, and β21 strands, which evidence suggests are proximal to the V3 loop in unliganded gp120, also resulted in decreased gp120-gp41 association. Thus, a gp120 element composed of the V3 loop and adjacent beta strands contributes to quaternary interactions that stabilize the unliganded trimer. CD4 binding dismantles this element, altering the gp120-gp41 relationship and rendering the hydrophobic patch in the V3 tip available for chemokine receptor binding.

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