scholarly journals The HIV-1 Envelope Glycoprotein C3/V4 Region Defines a Prevalent Neutralization Epitope following Immunization

Cell Reports ◽  
2019 ◽  
Vol 27 (2) ◽  
pp. 586-598.e6 ◽  
Author(s):  
Lin Lei ◽  
Yuhe R. Yang ◽  
Karen Tran ◽  
Yimeng Wang ◽  
Chi-I Chiang ◽  
...  
Keyword(s):  
Envelope Glycoprotein ◽  
Neutralization Epitope ◽  
Hiv 1

scholarly journals Cryptic Nature of a Conserved, CD4-Inducible V3 Loop Neutralization Epitope in the Native Envelope Glycoprotein Oligomer of CCR5-Restricted, but Not CXCR4-Using, Primary Human Immunodeficiency Virus Type 1 Strains

2005 ◽  
Vol 79 (11) ◽  
pp. 6957-6968 ◽  
Author(s):  
Paolo Lusso ◽  
Patricia L. Earl ◽  
Francesca Sironi ◽  
Fabio Santoro ◽  
Chiara Ripamonti ◽  
...  
Keyword(s):  
Human Immunodeficiency Virus ◽  
Human Immunodeficiency Virus Type ◽  
Virus Type ◽  
Envelope Glycoprotein ◽  
Coreceptor Usage ◽  
Neutralization Epitope ◽  
Subtype B ◽  
Immunodeficiency Virus ◽  
Hiv 1

ABSTRACT The external subunit of the human immunodeficiency virus type 1 (HIV-1) envelope glycoprotein (Env), gp120, contains conserved regions that mediate sequential interactions with two cellular receptor molecules, CD4 and a chemokine receptor, most commonly CCR5 or CXCR4. However, antibody accessibility to such regions is hindered by diverse protective mechanisms, including shielding by variable loops, conformational flexibility and extensive glycosylation. For the conserved neutralization epitopes hitherto described, antibody accessibility is reportedly unrelated to the viral coreceptor usage phenotype. Here, we characterize a novel, conserved gp120 neutralization epitope, recognized by a murine monoclonal antibody (MAb), D19, which is differentially accessible in the native HIV-1 Env according to its coreceptor specificity. The D19 epitope is contained within the third variable (V3) domain of gp120 and is distinct from those recognized by other V3-specific MAbs. To study the reactivity of MAb D19 with the native oligomeric Env, we generated a panel of PM1 cells persistently infected with diverse primary HIV-1 strains. The D19 epitope was conserved in the majority (23/29; 79.3%) of the subtype-B strains tested, as well as in selected strains from other genetic subtypes. Strikingly, in CCR5-restricted (R5) isolates, the D19 epitope was invariably cryptic, although it could be exposed by addition of soluble CD4 (sCD4); epitope masking was dependent on the native oligomeric structure of Env, since it was not observed with the corresponding monomeric gp120 molecules. By contrast, in CXCR4-using strains (X4 and R5X4), the epitope was constitutively accessible. In accordance with these results, R5 isolates were resistant to neutralization by MAb D19, becoming sensitive only upon addition of sCD4, whereas CXCR4-using isolates were neutralized regardless of the presence of sCD4. Other V3 epitopes examined did not display a similar divergence in accessibility based on coreceptor usage phenotype. These results provide the first evidence of a correlation between HIV-1 biological phenotype and neutralization sensitivity, raising the possibility that the in vivo evolution of HIV-1 coreceptor usage may be influenced by the selective pressure of specific host antibodies.

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

Specificity of Chimpanzee Antibodies Binding a Strain‐Specific HIV‐1 Neutralization Epitope of the External Envelope

1989 ◽  
Vol 18 (3-4) ◽  
pp. 357-362
Author(s):  
Jaap Goudsmit ◽  
Margreet Bakker ◽  
Lia Smit ◽  
Rob H. Meloen
Keyword(s):  
Neutralization Epitope ◽  
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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