Galectin-1 acts as a soluble host factor that promotes HIV-1 infectivity through stabilization of virus attachment to host cells
| Autor: | Jun Hirabayashi, Michel Ouellet, Michel J. Tremblay, Sachiko Sato, Simon Mercier, Salim Bounou, Isabelle Pelletier, Jocelyn Roy |
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| Rok vydání: | 2005 |
| Předmět: |
Stromal cell
Galectin 1 Galectin 3 Immunology Cell HIV Infections Plasma protein binding Biology Biological Factors medicine Cell Adhesion Immunology and Allergy Humans Tissue Distribution Cell adhesion Cells Cultured Host factor Infectivity virus diseases Cell biology medicine.anatomical_structure Solubility Galectin-1 HIV-1 CD8 Protein Binding |
| Zdroj: | Journal of immunology (Baltimore, Md. : 1950). 174(7) |
| ISSN: | 0022-1767 |
| Popis: | The establishment of HIV type 1 (HIV-1) infection is initiated by the stable attachment of the virion to the target cell surface. Although this process relies primarily upon interaction between virus-encoded gp120 and cell surface CD4, a number of distinct interactions influence binding of HIV-1 to host cells. In this study, we report that galectin-1, a dimeric β-galactoside-binding protein, promotes infection with R5, X4, and R5X4 variants. Galectin-1 acts as a soluble adhesion molecule by facilitating attachment of HIV-1 to the cell surface. This postulate is based on experiments where galectin-1 rendered HIV-1 particles more refractory to various agents that block HIV-1 adsorption and coreceptor binding (i.e., a blocking anti-CD4, soluble CD4, human anti-HIV-1 polyclonal Abs; stromal cell-derived factor-1α; RANTES). Experiments performed with the fusion inhibitor T-20 confirmed that galectin-1 is primarily affecting HIV-1 attachment. The relevance of the present findings for the pathogenesis of HIV-1 infection is provided by the fact that galectin-1 is abundantly expressed in the thymus and lymph nodes, organs that represent major reservoirs for HIV-1. Moreover, galectin-1 is secreted by activated CD8+ T lymphocytes, which are found in high numbers in HIV-1-positive patients. Therefore, it is proposed that galectin-1, which is released in an exocrine fashion at HIV-1 replication sites, can cross-link HIV-1 and target cells and promote a firmer adhesion of the virus to the cell surface, thereby augmenting the efficiency of the infection process. Overall, our findings suggest that galectin-1 might affect the pathogenesis of HIV-1 infection. |
| Databáze: | OpenAIRE |
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