4.7 Review

Bitter-sweet symphony: glycan-lectin interactions in virus biology

期刊

FEMS MICROBIOLOGY REVIEWS
卷 38, 期 4, 页码 598-632

出版社

OXFORD UNIV PRESS
DOI: 10.1111/1574-6976.12052

关键词

DC-SIGN; collectin; galectin; hemagglutinin; receptor-destroying enzyme; antiviral

资金

  1. Flemish Institute for the Promotion of Innovation by Science and Technology (I.W.T.-Flanders) [SB 61491, 63491]
  2. Special Research Fund of Ghent University
  3. Leibniz Gemeinschaft
  4. F.W.O.-Vlaanderen

向作者/读者索取更多资源

Glycans are carbohydrate modifications typically found on proteins or lipids, and can act as ligands for glycan-binding proteins called lectins. Glycans and lectins play crucial roles in the function of cells and organs, and in the immune system of animals and humans. Viral pathogens use glycans and lectins that are encoded by their own or the host genome for their replication and spread. Recent advances in glycobiological research indicate that glycans and lectins mediate key interactions at the virus-host interface, controlling viral spread and/or activation of the immune system. This review reflects on glycan-lectin interactions in the context of viral infection and antiviral immunity. A short introduction illustrates the nature of glycans and lectins, and conveys the basic principles of their interactions. Subsequently, examples are discussed highlighting specific glycan-lectin interactions and how they affect the progress of viral infections, either benefiting the host or the virus. Moreover, glycan and lectin variability and their potential biological consequences are discussed. Finally, the review outlines how recent advances in the glycan-lectin field might be transformed into promising new approaches to antiviral therapy.

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