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• W2007653463 abstract "Following primary infection with human immunodeficiency virus type-1 (HIV-1), macrophages are thought to play an important role, as they are one of the first target cells the virus encounters and can also sustain a significant production of viruses over extended periods of time. While the interaction between the primary cellular receptor CD4 and the virus-encoded external envelope glycoprotein gp120 initiates the infection process, it has been suggested that various host factors are exploited by HIV-1 to facilitate adsorption onto the cell surface. Macrophages and other cells found at the infection site can secrete a soluble mammalian lectin, galectin-1, which binds to β-galactoside residues through its carbohydrate recognition domain. Being a dimer, galectin-1 can cross-link ligands expressed on different constituents to mediate adhesion between cells or between cells and pathogens. We report here that galectin-1, but not galectin-3, increased HIV-1 infectivity in monocyte-derived macrophages (MDMs). This phenomenon was likely due to an enhancement of virus adsorption kinetics, which facilitates HIV-1 entry. The fusion inhibitors T-20 and TAK779 remained effective at reducing infection even in the presence of galectin-1, indicating that the galectin-1-mediated effect is occurring at a step prior to fusion. Together, our data suggest that galectin-1 can facilitate HIV-1 infection in MDMs by promoting early events of the virus replicative cycle (i.e. adsorption)." @default.
• W2007653463 created "2016-06-24" @default.
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• W2007653463 date "2008-02-01" @default.
• W2007653463 modified "2023-09-26" @default.
• W2007653463 title "Galectin-1 promotes HIV-1 infectivity in macrophages through stabilization of viral adsorption" @default.
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• W2007653463 doi "https://doi.org/10.1016/j.virol.2007.09.034" @default.
• W2007653463 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/18028978" @default.
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