Glycans, galectins, and HIV-1 infection

• Published in: Annals of the New York Academy of Sciences 2012-04, Vol.1253 (1), p.133-148
• Main Authors: Sato, Sachiko, Ouellet, Michel, St-Pierre, Christian, Tremblay, Michel J.
• Format: Article
• Language: English
• Subjects: CD4 Antigens - metabolism; galectin; Galectins - immunology; Galectins - metabolism; glycobiology; Glycosylation; HIV Envelope Protein gp120 - immunology; HIV Envelope Protein gp120 - metabolism; HIV Infections - etiology; HIV Infections - immunology; HIV Infections - metabolism; HIV-1; HIV-1 - immunology; HIV-1 - pathogenicity; HIV-1 - physiology; Host-Pathogen Interactions - immunology; Human immunodeficiency virus 1; Humans; Infections; lectin; Lectins, C-Type - immunology; Lectins, C-Type - metabolism; Models, Biological; Polysaccharides - immunology; Polysaccharides - metabolism; Virus Replication
• ISSN: 0077-8923; 1749-6632
• DOI: 10.1111/j.1749-6632.2012.06475.x

During sexual transmission, HIV‐1 must overcome physiological barriers to establish a founder cell population. Viral adhesion represents a bottleneck for HIV‐1 propagation that the virus widens by exploiting some specific host factors. Recognition of oligomannosyl glycans of gp120 by C‐type lectins is one such example. Recent works suggest that complex glycans of gp120 are recognized by another host lectin, galectin‐1. This interaction results in rapid association of HIV‐1 to susceptible cells and facilitates infection. The peculiar presentation of complex glycans on gp120 seems to impart specificity for galectin‐1, as another member of the same family, galectin‐3, is unable to bind gp120 or enhance HIV‐1 infection. Other studies have shown that galectin‐9 could also increase HIV‐1 infectivity but via an indirect mechanism. Thus, current research suggests that galectins play various roles in HIV‐1 pathogenesis. Drug discovery approaches targeting host lectins at early steps could benefit the current arsenal of antiretrovirals.