HIV-1 entry into CD4+ cells is mediated by the chemokine receptor CC-CKR-5

  title={HIV-1 entry into CD4+ cells is mediated by the chemokine receptor CC-CKR-5},
  author={Tatjana Dragic and Virginia M. Litwin and Graham Allaway and Scott R. Martin and Yaoxing Huang and Kirsten A. Nagashima and Charmagne S. Cayanan and Paul Jay Maddon and Richard A. Koup and John Percy Moore and William A. Paxton},
The β-chemokines MIP-1α, MIP-1β and RANTES inhibit infection of CD4+ cells by primary, non-syncytium-inducing (NSI) HIV-1 strains at the virus entry stage, and also block env-mediated cell–cell membrane fusion. CD4+ T cells from some HIV-1-exposed uninfected individuals cannot fuse with NSI HIV-1 strains and secrete high levels of β-chemokines. Expression of the β-chemokine receptor CC-CKR-5 in CD4+ , non-permissive human and non-human cells renders them susceptible to infection by NSI strains… 

CD4-independent utilization of the CXCR4 chemokine receptor by HIV-1 and HIV-2.

Acquisition of HIV type 1 resistance by beta-chemokine-producing CD4+ T cells.

The results suggest the presence of a clonal self-defense mechanism within the CD4+ T cell population in vivo that involves the secretion of beta-chemokines.

CD4-dependent, antibody-sensitive interactions between HIV-1 and its co-receptor CCR-5

CD4 binding, although not absolutely necessary for the gp120–CCR-5 interaction, greatly increases its efficiency, and interference with HIV-1 binding to one or both of its receptors (CD4 and CCR-5) may be an important mechanism of virus neutralization.

The CXC chemokine IP-10 stimulates HIV-1 replication

It is demonstrated that IP-10 stimulates HIV-1 replication in monocyte-derived macrophages and peripheral blood lymphocytes and that blocking the interaction betweenIP-10 and CXCR3 represents a possible new target for anti-retroviral therapy.

Differential regulation of HIV-1 fusion cofactor expression by CD28 costimulation of CD4+ T cells.

Activation of CD4(+) T lymphocytes from human immunodeficiency virus-type 1 (HIV-1)-infected donors with immobilized antibodies to CD3 and CD28 induces a virus-resistant state. This effect is

Role of beta-chemokines in HIV-1 infection of dendritic cells maturing from CD34+ stem cells.

In addition to the initial anti-M- Tropic virus effect by beta-chemokines, selective pressure on viruses may also result because of an increase in susceptibility to T-tropic virus.

Macrophage Inflammatory Protein 1α Inhibits Postentry Steps of Human Immunodeficiency Virus Type 1 Infection via Suppression of Intracellular Cyclic AMP

The data reveal that β-chemokine-mediated inhibition of virus replication in primary lymphocytes combines inhibitory effects at the entry and postentry levels and imply the involvement of β- Chemokines-induced signaling in postentry inhibition of HIV-1 infection.

In vivo evolution of HIV-1 co-receptor usage and sensitivity to chemokine-mediated suppression

A consistent pattern of evolution of viral co-receptor usage and sensitivity to chemokine-mediated suppression in a longitudinal follow-up of children with progressive HIV-1 infection is document.



Identification of RANTES, MIP-1α, and MIP-1β as the Major HIV-Suppressive Factors Produced by CD8+ T Cells

Recombinant human RANTES, Mip-1α, and MIP-1β induced a dose-dependent inhibition of different strains of HIV-1, HIV-2, and simian immunodeficiency virus (SIV) and may have relevance for the prevention and therapy of AIDS.

HIV-1 Entry Cofactor: Functional cDNA Cloning of a Seven-Transmembrane, G Protein-Coupled Receptor

A cofactor for HIV-1 (human immunodeficiency virus-type 1) fusion and entry was identified with the use of a novel functional complementary DNA (cDNA) cloning strategy that is a putative G protein-coupled receptor with seven transmembrane segments.

Growth of macrophage-tropic and primary human immunodeficiency virus type 1 (HIV-1) isolates in a unique CD4+ T-cell clone (PM1): failure to downregulate CD4 and to interfere with cell-line-tropic HIV-1

Resistent with the lack of CD4 downregulation, persistent infection of PM1 by HIV-1BaL or HIV-2(573) failed to interfere with HIV-3IIIB superinfection, suggesting that a direct viral interaction may occur in vivo between biologically diverse HIV- 1 strains.

Proteinase-resistant factors in human erythrocyte membranes mediate CD4-dependent fusion with cells expressing human immunodeficiency virus type 1 envelope glycoproteins

The role of human-specific factors in Env/CD4-mediated fusion is shown by the ability of transient cell hybrids formed between CD4+ murine cells and human HeLa cells to fuse with Env+ cells.

Vpr is required for efficient replication of human immunodeficiency virus type-1 in mononuclear phagocytes.

It is shown that vpr is important for efficient viral replication in primary monocyte/macrophages, but appears to play no role in activated or resting T cell infection, and a role for vpr molecules produced in newly infected cells is suggested, in addition to its presumed function in the virion.

Heat-resistant factors in human erythrocyte membranes mediate CD4-dependent fusion with cells expressing HIV-1 envelope glycoproteins.

Human red blood cells (huRBC) was used as a source for the accessory components since their membrane composition is less complex than that of nucleated cells and they are well characterized and they supported HIV-1 envelope glycoprotein-mediated fusion.

Cloning and Functional Expression of a Human Eosinophil CC Chemokine Receptor (*)

CC CKR3 may be one of the host factors responsible for selective recruitment of eosinophils to sites of inflammation, and is a seven-transmembrane domain G protein-coupled receptor most closely related to the previously reported monocyte- and neutrophil-selective receptor CC CKR1.

Activation of dual T cell signaling pathways by the chemokine RANTES.

In addition to inducing chemotaxis, RANTES can act as an antigen-independent activator of T cells in vitro, and was associated with a spectrum of cellular responses--Ca2+ channel opening, interleukin-2 receptor expression, cytokine release, and T cell proliferation--characteristic of T cell receptor activation.