Glycosylation of Human IgA Directly Inhibits Influenza A and Other Sialic-Acid-Binding Viruses
| Autor: | Lars Hangartner, Larissa Meyer, V. Orlowski, Arkadiusz Wyrzucki, Ngoc Phuong Lan Le, Matteo Bianchi, Hannah L. Turner, Marco Steck, Andrew B. Ward, Max Crispin, Michael A. Maurer |
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| Jazyk: | angličtina |
| Rok vydání: | 2018 |
| Předmět: |
0301 basic medicine
Immunoglobulin A Glycosylation neuraminidase Chick Embryo Sialic acid binding Article influenza virus General Biochemistry Genetics and Molecular Biology Madin Darby Canine Kidney Cells Microbiology 03 medical and health sciences chemistry.chemical_compound Dogs 0302 clinical medicine Viral envelope Chlorocebus aethiops antibodies Animals Humans innate immunity Vero Cells lcsh:QH301-705.5 heterosubtypic antibodies Innate immune system biology Chemistry Immunity Innate N-Acetylneuraminic Acid 3. Good health Sialic acid carbohydrates (lipids) HEK293 Cells 030104 developmental biology lcsh:Biology (General) Influenza A virus virus neutralization biology.protein mucosal immunity Antibody immunoglobulin Protein Processing Post-Translational Breast feeding Neuraminidase IgA Protein Binding 030215 immunology |
| Zdroj: | Cell Reports, Vol 23, Iss 1, Pp 90-99 (2018) Cell Reports |
| ISSN: | 2211-1247 |
| Popis: | Summary Immunoglobulin A (IgA) plays an important role in protecting our mucosal surfaces from viral infection, in maintaining a balance with the commensal bacterial flora, and in extending maternal immunity via breast feeding. Here, we report an additional innate immune effector function of human IgA molecules in that we demonstrate that the C-terminal tail unique to IgA molecules interferes with cell-surface attachment of influenza A and other enveloped viruses that use sialic acid as a receptor. This antiviral activity is mediated by sialic acid found in the complex N-linked glycans at position 459. Antiviral activity was observed even in the absence of classical antibody binding via the antigen binding sites. Our data, therefore, show that the C-terminal tail of IgA subtypes provides an innate line of defense against viruses that use sialic acid as a receptor and the role of neuraminidases present on these virions. Graphical Abstract Highlights • Heterosubtypic IgA1 or IgA2 antibodies neutralize virus much more potently than IgG1 • Sialic acid in IgA’s C-terminal tail competes with viral receptor binding • This may represent an innate line of defense against viral pathogens Vertebrate IgA molecules possess a conserved N-linked glycosylated C-terminal tail. Maurer et al. show that sialic acid found in the complex glycosylation of the C-terminal tail of human IgA1 inhibits sialic-acid-binding viruses and, therefore, may constitute an additional line of innate immunity. |
| Databáze: | OpenAIRE |
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