scholarly journals HIV-1 Entry and Macrophage Inflammatory Protein-1β-mediated Signaling Are Independent Functions of the Chemokine Receptor CCR5

1997 ◽  
Vol 272 (11) ◽  
pp. 6854-6857 ◽  
Author(s):  
Michael Farzan ◽  
Hyeryun Choe ◽  
Kathleen A. Martin ◽  
Ying Sun ◽  
Mary Sidelko ◽  
...  
Keyword(s):  
Chemokine Receptor ◽  
Inflammatory Protein ◽  
Independent Functions ◽  
Chemokine Receptor Ccr5 ◽  
Macrophage Inflammatory Protein ◽  
Hiv 1 ◽  
Receptor Ccr5

Down-regulation of the chemokine receptor CCR5 by activation of chemotactic formyl peptide receptor in human monocytes

Blood ◽  
2000 ◽  
Vol 96 (8) ◽  
pp. 2887-2894 ◽  
Author(s):  
Weiping Shen ◽  
Baoqun Li ◽  
Michele A. Wetzel ◽  
Thomas J. Rogers ◽  
Earl E. Henderson ◽  
...  
Keyword(s):  
Chemokine Receptor ◽  
Regulatory Elements ◽  
Serine Phosphorylation ◽  
Formyl Peptide Receptor ◽  
Down Regulation ◽  
Peptide Receptor ◽  
Formyl Peptide ◽  
Chemokine Receptor Ccr5 ◽  
Hiv 1 ◽  
Receptor Ccr5

Abstract Interactions between cell surface receptors are important regulatory elements in the complex host responses to infections. In this study, it is shown that a classic chemotactic factor, the bacterial chemotactic peptide N-formyl-methionyl-leucylphenyl-alanine (fMLF), rapidly induced a protein-kinase-C–mediated serine phosphorylation and down-regulation of the chemokine receptor CCR5, which serves as a major human immunodeficiency virus (HIV)-1 coreceptor. The fMLF binding to its receptor, formyl peptide receptor (FPR), resulted in significant attenuation of cell responses to CCR5 ligands and in inhibition of HIV-1-envelope-glycoprotein–mediated fusion and infection of cells expressing CD4, CCR5, and FPR. The finding that the expression and function of CCR5 can be regulated by peptides that use an unrelated receptor may provide a novel approach to the design of anti-inflamatory and antiretroviral agents.

Susceptibility of pediatric HIV-1 isolates to recombinant CD4-IgG2 (PRO 542) and humanized mAb to the chemokine receptor CCR5 (PRO 140)

2006 ◽  
Vol 118 (2) ◽  
pp. 518-521 ◽  
Author(s):  
William T. Shearer ◽  
Jaime G. DeVille ◽  
Pearl M. Samson ◽  
John H. Moye Jr. ◽  
Courtney V. Fletcher ◽  
...  
Keyword(s):  
Chemokine Receptor ◽  
Pediatric Hiv ◽  
Chemokine Receptor Ccr5 ◽  
Hiv 1 ◽  
Receptor Ccr5

scholarly journals Synthesis of Peptides Mimicking Chemokine Receptor CCR5 and Their Inhibitory Effects against HIV-1 Infection.

2000 ◽  
Vol 48 (2) ◽  
pp. 308-309 ◽  
Author(s):  
Koji KONISHI ◽  
Kiyoshi IKEDA ◽  
Kazuo ACHIWA ◽  
Hiroo HOSHINO ◽  
Kiyoshi TANAKA
Keyword(s):  
Chemokine Receptor ◽  
Inhibitory Effects ◽  
Chemokine Receptor Ccr5 ◽  
Hiv 1 ◽  
Receptor Ccr5

scholarly journals Frequency of the CCR5-delta 32 chemokine receptor gene mutation in the Lebanese population

2004 ◽  
Vol 10 (4-5) ◽  
pp. 671-675
Author(s):  
W. Karam ◽  
R. Jurjus ◽  
N. Khoury ◽  
H. Khansa ◽  
C. Assad ◽  
...  
Keyword(s):  
Chemokine Receptor ◽  
Educational Level ◽  
Receptor Gene ◽  
Northern Europe ◽  
Ccr5 Gene ◽  
Lebanese Population ◽  
Chemokine Receptor Ccr5 ◽  
Hiv 1 ◽  
Receptor Ccr5 ◽  
Chemokine Receptor Gene

A direct correlation between HIV infection and mutation in the chemokine receptor [CCR5] gene has been established. However, such correlation has never been investigated in Lebanon. We report the frequency of the CCR5-delta 32 mutation in a r and om sample of 209 healthy, HIV-1 seronegative Lebanese aged 19-68. Overall, 4.8% were heterozygous for the mutation. Homozygosity was absent from our sample. The frequency for the CCR5-delta 32 allele was 2.5%. Distribution of the mutation was unaffected by sex, age, religion or educational level. The frequency in the Lebanese population is consistent with that in the origin of the mutation in northern Europe. This could be attributed to a gene flow into the Middle East from northern Europe

Down-regulation of the chemokine receptor CCR5 by activation of chemotactic formyl peptide receptor in human monocytes

Blood ◽  
2000 ◽  
Vol 96 (8) ◽  
pp. 2887-2894
Author(s):  
Weiping Shen ◽  
Baoqun Li ◽  
Michele A. Wetzel ◽  
Thomas J. Rogers ◽  
Earl E. Henderson ◽  
...  
Keyword(s):  
Chemokine Receptor ◽  
Regulatory Elements ◽  
Serine Phosphorylation ◽  
Formyl Peptide Receptor ◽  
Down Regulation ◽  
Peptide Receptor ◽  
Formyl Peptide ◽  
Chemokine Receptor Ccr5 ◽  
Hiv 1 ◽  
Receptor Ccr5

Interactions between cell surface receptors are important regulatory elements in the complex host responses to infections. In this study, it is shown that a classic chemotactic factor, the bacterial chemotactic peptide N-formyl-methionyl-leucylphenyl-alanine (fMLF), rapidly induced a protein-kinase-C–mediated serine phosphorylation and down-regulation of the chemokine receptor CCR5, which serves as a major human immunodeficiency virus (HIV)-1 coreceptor. The fMLF binding to its receptor, formyl peptide receptor (FPR), resulted in significant attenuation of cell responses to CCR5 ligands and in inhibition of HIV-1-envelope-glycoprotein–mediated fusion and infection of cells expressing CD4, CCR5, and FPR. The finding that the expression and function of CCR5 can be regulated by peptides that use an unrelated receptor may provide a novel approach to the design of anti-inflamatory and antiretroviral agents.

Cholesterol is essential for macrophage inflammatory protein 1β binding and conformational integrity of CC chemokine receptor 5

Blood ◽  
2002 ◽  
Vol 99 (12) ◽  
pp. 4298-4306 ◽  
Author(s):  
Dzung H. Nguyen ◽  
Dennis Taub
Keyword(s):  
Lipid Rafts ◽  
Chemokine Receptor ◽  
Membrane Microdomains ◽  
Inflammatory Protein ◽  
Immunodeficiency Virus ◽  
Chemokine Receptor Ccr5 ◽  
And Function ◽  
Cc Chemokine Receptor 5 ◽  
Macrophage Inflammatory Protein

The chemokine receptor, CCR5, is used as a human immunodeficiency virus coreceptor in combination with CD4 during transmission and early infection. CCR5 has been shown to be palmitoylated and targeted to cholesterol- and sphingolipid-rich membrane microdomains termed “lipid rafts.” However, the role of cholesterol and lipid rafts on chemokine binding and signaling through CCR5 remains unknown. We found that cholesterol extraction by hydroxypropyl-β-cyclodextrin (BCD) significantly reduced the binding and signaling of macrophage inflammatory protein 1β (MIP-1β) using CCR5-expressing CEM-NKR T cells. Reloading treated cells with cholesterol but not 4-cholesten-3-one, an oxidized form of cholesterol, restored MIP-1β binding to BCD-treated cells. Antibodies specific for distinct CCR5 epitopes lost their ability to bind to the cell surface after cholesterol extraction to varying degrees. Moreover, cells stained with fluorescently labeled MIP-1β extensively colocalized with the GM1 lipid raft marker while using anti-CCR5 antibodies; most of CCR5 on these cells only partially colocalized with GM1, suggesting that active ligand binding facilitates receptor association with lipid rafts or that raft association promotes a higher affinity conformation of CCR5. Together, these data demonstrate that cholesterol and lipid rafts are important for the maintenance of the CCR5 conformation and are necessary for both the binding and function of this chemokine receptor.

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