Abstract
Glycan–lectin interactions play an essential role in different cellular processes. One of their main functions is involvement in the immune response to pathogens or inflammation. However, cancer cells and viruses have adapted to avail themselves of these interactions. By displaying specific glycosylation structures, they are able to bind to lectins, thus promoting pathogenesis. While glycan–lectin interactions promote tumor progression, metastasis, and/or chemoresistance in cancer, in viral infections they are important for viral entry, release, and/or immune escape. For several years now, a growing number of investigations have been devoted to clarifying the role of glycan–lectin interactions in cancer and viral infections. Various overviews have already summarized and highlighted their findings. In this review, we consider the interactions of the lectins MGL, DC-SIGN, selectins, and galectins in both cancer and viral infections together. A possible transfer of ways to target and disrupt them might lead to new therapeutic approaches in different pathological backgrounds.
Highlights
Glycosylation is a multistep process involving the covalent addition of saccharides to proteins or lipids at the endoplasmic reticulum and Golgi
dendritic cell-specific intracellular adhesion molecule 3-grabbing nonintegrin (DC-SIGN) interacts, mainly with the highly expressed Lewis glyco-epitopes. This lectin detects a wide range of viral glycoproteins, including high-mannose residues on the gp120 of human immunodeficiency virus (HIV), high-mannose glycans of Ebola virus (EBOV), as well as high-mannose and Le epitopes on the spike protein of SARS-CoV-2. (c) Selectins are found on endothelial cells, platelets, and leukocytes and recognize sialyl Le antigen x and its isomer sialyl Le antigen a
DC-SIGN is well known for binding mannose-rich carbohydrates [61] that are present on the surface of filoviruses [100,101], in the mucin domain of GP1, a subunit of the GP, on the Ebola virus
Summary
We will focus on the interactions of glycans with four different lectins, namely galectins and three different C-type lectin receptors (CLRs) including the macrophage galactose binding lectin (MGL), the dendritic cell-specific intracellular adhesion molecule 3-grabbing nonintegrin (DC-SIGN), and selectins. 2021, 22, x FOR PEER REVIEW lectins because it has been shown that all four receptors play a key role in cancer [6,7] and in viral infection [8,9] by interacting with disease-specific glycosylation patterns. We describe the role of lectins interacting with glycan patterns or GPs of well-known viruses including human immunodeficiency virus (HIV), Ebola virus (EBOV), influenza virus, and the severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) We show their role in promoting infection and discuss potential therapeutic strategies. Such commonalities could be the basis for further investigations with the goal of translating promising therapeutic approaches in either cancer or viral infections to the other disease
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