Binding of HTLV-1 virions to T cells occurs by a temperature and calcium-dependent process and is blocked by certain type 2 adenosine receptor antagonists
| Autor: | Thomas J. Kindt, Bishop F. Hague, Tong Mao Zhao |
|---|---|
| Rok vydání: | 2003 |
| Předmět: |
Cancer Research
Adenosine 2-Chloroadenosine Cations Divalent medicine.drug_class T-Lymphocytes viruses chemistry.chemical_element Adenosine-5'-(N-ethylcarboxamide) Calcium Biology Cleavage (embryo) Monoclonal antibody Virus Divalent Membrane Microdomains Virology Phenethylamines Purinergic P1 Receptor Agonists medicine Humans Lipid raft Cell Line Transformed chemistry.chemical_classification Human T-lymphotropic virus 1 Antibodies Monoclonal Triazoles Molecular biology Adenosine receptor Kinetics Infectious Diseases chemistry Quinazolines biology.protein Thermodynamics Antibody |
| Zdroj: | Virus Research. 93:31-39 |
| ISSN: | 0168-1702 |
| DOI: | 10.1016/s0168-1702(03)00048-0 |
| Popis: | A flow cytometric assay that measures binding of human T-lymphotropic virus type 1 (HTLV-1) virions to target cells was used to investigate the binding process and to screen for compounds affecting viral binding. Results showed that adenosine receptor type 2 antagonists effectively inhibit viral binding at concentrations below 10 microM; no inhibition was seen when antagonist was used to pretreat cells or was added post binding, suggesting direct interference with virus attachment. Efficient HTLV-1 binding required divalent calcium ions and temperatures greater than 20 degrees C. Disruption of lipid rafts by cholesterol depletion compromised viral binding but cleavage of glycosyl-phosphatidylinositol linkages had no effect. A monoclonal antibody (mAb) that recognizes HTLV-1 envelope positions 190-209 impaired binding of virus while other anti-envelope antibodies had no effect. These findings place major constraints on the nature of the HTLV-1 cell binding process and identify a class of inhibitors that may have potential for treatment of infection. |
| Databáze: | OpenAIRE |
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