scholarly journals A Novel Synthetic Bivalent Ligand To Probe Chemokine Receptor CXCR4 Dimerization and Inhibit HIV-1 Entry

Biochemistry ◽  
2012 ◽  
Vol 51 (36) ◽  
pp. 7078-7086 ◽  
Author(s):  
Won-Tak Choi ◽  
Santhosh Kumar ◽  
Navid Madani ◽  
Xiaofeng Han ◽  
Shaomin Tian ◽  
...  
Keyword(s):  
Chemokine Receptor ◽  
Bivalent Ligand ◽  
Chemokine Receptor Cxcr4 ◽  
Hiv 1

scholarly journals Bivalent Ligand Aiming Putative Mu Opioid Receptor and Chemokine Receptor CXCR4 Dimers in Opioid Enhanced HIV-1 Entry

2020 ◽  
Vol 11 (11) ◽  
pp. 2318-2324
Author(s):  
Hongguang Ma ◽  
Huiqun Wang ◽  
Mengchu Li ◽  
Victor Barreto-de-Souza ◽  
Bethany A. Reinecke ◽  
...  
Keyword(s):  
Opioid Receptor ◽  
Chemokine Receptor ◽  
Mu Opioid Receptor ◽  
Bivalent Ligand ◽  
Mu Opioid ◽  
Chemokine Receptor Cxcr4 ◽  
Hiv 1

HIV-1 gp120 enhances giant depolarizing potentials via chemokine receptor CXCR4 in neonatal rat hippocampus

2006 ◽  
Vol 23 (5) ◽  
pp. 1120-1128 ◽  
Author(s):  
Alexander Kasyanov ◽  
Hirokazu Tamamura ◽  
Nobutaka Fujii ◽  
Huangui Xiong
Keyword(s):  
Chemokine Receptor ◽  
Rat Hippocampus ◽  
Neonatal Rat ◽  
Chemokine Receptor Cxcr4 ◽  
Hiv 1

scholarly journals A Small-molecule Inhibitor Directed against the Chemokine Receptor CXCR4 Prevents its Use as an HIV-1 Coreceptor

1997 ◽  
Vol 186 (8) ◽  
pp. 1395-1400 ◽  
Author(s):  
Benjamin J. Doranz ◽  
Kathie Grovit-Ferbas ◽  
Matthew P. Sharron ◽  
Si-Hua Mao ◽  
Matthew Bidwell Goetz ◽  
...  
Keyword(s):  
Membrane Fusion ◽  
Small Molecule ◽  
Chemokine Receptor ◽  
Viral Entry ◽  
Small Molecule Inhibitor ◽  
Chemokine Receptor Cxcr4 ◽  
Mechanism Of Inhibition ◽  
Molecule Inhibitor ◽  
Immunodeficiency Virus ◽  
Hiv 1

The chemokine receptor CXCR4 is the major coreceptor used for cellular entry by T cell– tropic human immunodeficiency virus (HIV)-1 strains, whereas CCR5 is used by macrophage (M)-tropic strains. Here we show that a small-molecule inhibitor, ALX40-4C, inhibits HIV-1 envelope (Env)-mediated membrane fusion and viral entry directly at the level of coreceptor use. ALX40-4C inhibited HIV-1 use of the coreceptor CXCR4 by T- and dual-tropic HIV-1 strains, whereas use of CCR5 by M- and dual-tropic strains was not inhibited. Dual-tropic viruses capable of using both CXCR4 and CCR5 were inhibited by ALX40-4C only when cells expressed CXCR4 alone. ALX40-4C blocked stromal-derived factor (SDF)-1α–mediated activation of CXCR4 and binding of the monoclonal antibody 12G5 to cells expressing CXCR4. Overlap of the ALX40-4C binding site with that of 12G5 and SDF implicates direct blocking of Env interactions, rather than downregulation of receptor, as the mechanism of inhibition. Thus, ALX40-4C represents a small-molecule inhibitor of HIV-1 infection that acts directly against a chemokine receptor at the level of Env-mediated membrane fusion.

The implication of the chemokine receptor CXCR4 in HIV-1 envelope protein-induced apoptosis is independent of the G protein-mediated signalling

AIDS ◽  
1999 ◽  
Vol 13 (8) ◽  
pp. 909-917 ◽  
Author(s):  
Julià Blanco ◽  
Etienne Jacotot ◽  
Cecilia Cabrera ◽  
Ana Cardona ◽  
Bonaventura Clotet ◽  
...  
Keyword(s):  
G Protein ◽  
Chemokine Receptor ◽  
Envelope Protein ◽  
Chemokine Receptor Cxcr4 ◽  
Induced Apoptosis ◽  
Hiv 1

The Effect of Early HIV-1 Infection on Expression and Function of the Chemokine Receptor CXCR4

2000 ◽  
Vol 28 (1) ◽  
pp. A30-A30
Author(s):  
Brendan J. Murphy ◽  
Richard Q. Zheng ◽  
Keith E. Nye
Keyword(s):  
Chemokine Receptor ◽  
Chemokine Receptor Cxcr4 ◽  
And Function ◽  
Hiv 1

scholarly journals Design and synthesis of a bivalent probe targeting the putative mu opioid receptor and chemokine receptor CXCR4 heterodimer

2020 ◽  
Vol 11 (1) ◽  
pp. 125-131 ◽  
Author(s):  
Bethany A. Reinecke ◽  
Guifeng Kang ◽  
Yi Zheng ◽  
Samuel Obeng ◽  
Huijun Zhang ◽  
...  
Keyword(s):  
Opioid Receptor ◽  
Chemokine Receptor ◽  
Mu Opioid Receptor ◽  
Bivalent Ligand ◽  
Mu Opioid ◽  
Design And Synthesis ◽  
Chemokine Receptor Cxcr4

The first bivalent ligand targeting the putative heterodimer of the mu opioid receptor and the chemokine receptor CXCR4.

Synthesis and Structure−Activity Relationships of Phenylenebis(methylene)- Linked Bis-azamacrocycles That Inhibit HIV-1 and HIV-2 Replication by Antagonism of the Chemokine Receptor CXCR4

1999 ◽  
Vol 42 (19) ◽  
pp. 3971-3981 ◽  
Author(s):  
Gary J. Bridger ◽  
Renato T. Skerlj ◽  
Sreenivasan Padmanabhan ◽  
Stephen A. Martellucci ◽  
Geoffrey W. Henson ◽  
...  
Keyword(s):  
Chemokine Receptor ◽  
Structure Activity Relationships ◽  
Chemokine Receptor Cxcr4 ◽  
Structure Activity ◽  
Hiv 1

scholarly journals Shared Usage of the Chemokine Receptor CXCR4 by Primary and Laboratory-Adapted Strains of Feline Immunodeficiency Virus

1999 ◽  
Vol 73 (5) ◽  
pp. 3661-3671 ◽  
Author(s):  
Jennifer Richardson ◽  
Gianfranco Pancino ◽  
Rastine Merat ◽  
Thierry Leste-Lasserre ◽  
Anne Moraillon ◽  
...  
Keyword(s):  
Chemokine Receptor ◽  
Feline Immunodeficiency Virus ◽  
Type I ◽  
Dependent Manner ◽  
Amino Terminal ◽  
Species Origin ◽  
Chemokine Receptor Cxcr4 ◽  
Immunodeficiency Virus ◽  
Hiv 1

ABSTRACT Strains of the feline immunodeficiency virus (FIV) presently under investigation exhibit distinct patterns of in vitro tropism. In particular, the adaptation of FIV for propagation in Crandell feline kidney (CrFK) cells results in the selection of strains capable of forming syncytia with cell lines of diverse species origin. The infection of CrFK cells by CrFK-adapted strains appears to require the chemokine receptor CXCR4 and is inhibited by its natural ligand, stromal cell-derived factor 1α (SDF-1α). Here we found that inhibitors of CXCR4-mediated infection by human immunodeficiency virus type I (HIV-1), such as the bicyclam AMD3100 and short peptides derived from the amino-terminal region of SDF-1α, also blocked infection of CrFK by FIV. Nevertheless, we observed differences in the ranking order of the peptides as inhibitors of FIV and HIV-1 and showed that such differences are related to the species origin of CXCR4 and not that of the viral envelope. These results suggest that, although the envelope glycoproteins of FIV and HIV-1 are substantially divergent, FIV and HIV-1 interact with CXCR4 in a highly similar manner. We have also addressed the role of CXCR4 in the life cycle of primary isolates of FIV. Various CXCR4 ligands inhibited infection of feline peripheral blood mononuclear cells (PBMC) by primary FIV isolates in a concentration-dependent manner. These ligands also blocked the viral transduction of feline PBMC by pseudotyped viral particles when infection was mediated by the envelope glycoprotein of a primary FIV isolate but not by the G protein of vesicular stomatitis virus, indicating that they act at an envelope-mediated step and presumably at viral entry. These findings strongly suggest that primary and CrFK-adapted strains of FIV, despite disparate in vitro tropisms, share usage of CXCR4.

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