Abstract
Galectins form a diverse but relatively conserved family of soluble β-galactoside-binding proteins. Their minimal binding glycan unit is β-galactoside residue, such as N-acetyllactosamine (Gal β1 - 4GlcNAc) found on N-linked glycans of surface proteins, but the steric environment and unique substitutions of the lactosamine residues greatly affect each galectin’s binding specificity. Some galectins can enhance the binding of pathogens to target cells. Galectin-1, for example, increases the binding of human immunodeficiency virus type 1 (HIV-1) to its natural targets, CD4+ T cells and macrophages. HIV-1 leads to a gradual decline of immune defenses and is the causative agent of acquired immunodeficiency syndrome (AIDS). Compared to other sexually transmitted viruses, transmission of HIV-1 generally requires a higher viral load and is rather inefficient. A significant bottleneck to transmission occurs at the immediate early contact of HIV-1 with the genital mucosa where target cells are found. The presence of galectin-1 in the intestinal and genital mucosa may be exploited by HIV-1 to enhance its potential at establishing a successful infection. Specific inhibition of galectin-1 could thus represent an interesting strategy to further reduce the occurrence of HIV-1 transmission.
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© 2014 Springer Japan
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Ouellet, M., Tremblay, M.J., Sato, S. (2014). HIV and Galectins. In: Endo, T., Seeberger, P., Hart, G., Wong, CH., Taniguchi, N. (eds) Glycoscience: Biology and Medicine. Springer, Tokyo. https://doi.org/10.1007/978-4-431-54836-2_150-1
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DOI: https://doi.org/10.1007/978-4-431-54836-2_150-1
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Publisher Name: Springer, Tokyo
Online ISBN: 978-4-431-54836-2
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