Article ; Online: Roles of Glycans and Non-glycans on the Epithelium and in the Immune System in H1-H18 Influenza A Virus Infections.
Methods in molecular biology (Clifton, N.J.)
2022 Volume 2556, Page(s) 205–242
Abstract: The large variation of influenza A viruses (IAVs) in various susceptible hosts and their rapid evolution, which allows host/tissue switching, host immune escape, vaccine escape, and drug resistance, are difficult challenges for influenza control in all ... ...
| Abstract | The large variation of influenza A viruses (IAVs) in various susceptible hosts and their rapid evolution, which allows host/tissue switching, host immune escape, vaccine escape, and drug resistance, are difficult challenges for influenza control in all countries worldwide. Access and binding of the IAV to actual receptors at endocytic sites is critical for the establishment of influenza infection. In this chapter, the progress in identification of and roles of glycans and non-glycans on the epithelium and in the immune system in H1-H18 IAV infections are reviewed. The first part of the review is on current knowledge of H1-H16 IAV receptors on the epithelium including sialyl glycans, other negatively charged glycans, and annexins. The second part of the review focuses on H1-H16 IAV receptors in the immune system including acidic surfactant phospholipids, Sia on surfactant proteins, the carbohydrate recognition domain (CRD) of surfactant proteins, Sia on mucins, Sia and C-type lectins on macrophages and dendritic cells, and Sia on NK cells. The third part of the review is about a possible H17-H18 IAV receptor. Binding of these receptors to IAVs may result in inhibition or enhancement of IAV infection depending on their location, host cell type, and IAV strain. Among these receptors, host sialyl glycans are key determinants of viral hemagglutinin (HA) lectins for H1-H16 infections. HA must acquire mutations to bind to sialyl glycans that are dominant on a new target tissue when switching to a new host for efficient transmission and to bind to long sialyl glycans found in the case of seasonal HAs with multiple glycosylation sites as a consequence of immune evasion. Although sialyl receptors/C-type lectins on immune cells are decoy receptors/pathogen recognition receptors for capturing viral HA lectin/glycans protecting HA antigenic sites, some IAV strains do not escape, such as by release with neuraminidase, but hijack these molecules to gain entry and replication in immune cells. An understanding of the virus-host battle tactics at the receptor level might lead to the establishment of novel strategies for effective control of influenza. |
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| MeSH term(s) | Epithelium ; Hemagglutinins, Viral ; Humans ; Influenza A virus ; Influenza Vaccines ; Influenza, Human ; Lectins, C-Type ; Macrophages ; Mucins ; Neuraminidase ; Polysaccharides |
| Chemical Substances | Hemagglutinins, Viral ; Influenza Vaccines ; Lectins, C-Type ; Mucins ; Polysaccharides ; Neuraminidase (EC 3.2.1.18) |
| Language | English |
| Publishing date | 2022-09-29 |
| Publishing country | United States |
| Document type | Journal Article ; Review |
| ISSN | 1940-6029 |
| ISSN (online) | 1940-6029 |
| DOI | 10.1007/978-1-0716-2635-1_16 |
| Database | MEDical Literature Analysis and Retrieval System OnLINE |
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