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Glycosylation of Human IgA Directly Inhibits Influenza A and Other Sialic-Acid-Binding Viruses

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 molec...

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Autores principales: Maurer, Michael A., Meyer, Larissa, Bianchi, Matteo, Turner, Hannah L., Le, Ngoc P.L., Steck, Marco, Wyrzucki, Arkadiusz, Orlowski, Vanessa, Ward, Andrew B., Crispin, Max, Hangartner, Lars
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Cell Press 2018
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5905402/
https://www.ncbi.nlm.nih.gov/pubmed/29617676
http://dx.doi.org/10.1016/j.celrep.2018.03.027
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author Maurer, Michael A.
Meyer, Larissa
Bianchi, Matteo
Turner, Hannah L.
Le, Ngoc P.L.
Steck, Marco
Wyrzucki, Arkadiusz
Orlowski, Vanessa
Ward, Andrew B.
Crispin, Max
Hangartner, Lars
author_facet Maurer, Michael A.
Meyer, Larissa
Bianchi, Matteo
Turner, Hannah L.
Le, Ngoc P.L.
Steck, Marco
Wyrzucki, Arkadiusz
Orlowski, Vanessa
Ward, Andrew B.
Crispin, Max
Hangartner, Lars
author_sort Maurer, Michael A.
collection PubMed
description 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.
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spelling pubmed-59054022018-04-19 Glycosylation of Human IgA Directly Inhibits Influenza A and Other Sialic-Acid-Binding Viruses Maurer, Michael A. Meyer, Larissa Bianchi, Matteo Turner, Hannah L. Le, Ngoc P.L. Steck, Marco Wyrzucki, Arkadiusz Orlowski, Vanessa Ward, Andrew B. Crispin, Max Hangartner, Lars Cell Rep Article 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. Cell Press 2018-04-05 /pmc/articles/PMC5905402/ /pubmed/29617676 http://dx.doi.org/10.1016/j.celrep.2018.03.027 Text en Crown Copyright © 2018 Published by Elsevier Inc. All rights reserved. http://creativecommons.org/licenses/by/4.0/ This is an open access article under the CC BY license (http://creativecommons.org/licenses/by/4.0/).
spellingShingle Article
Maurer, Michael A.
Meyer, Larissa
Bianchi, Matteo
Turner, Hannah L.
Le, Ngoc P.L.
Steck, Marco
Wyrzucki, Arkadiusz
Orlowski, Vanessa
Ward, Andrew B.
Crispin, Max
Hangartner, Lars
Glycosylation of Human IgA Directly Inhibits Influenza A and Other Sialic-Acid-Binding Viruses
title Glycosylation of Human IgA Directly Inhibits Influenza A and Other Sialic-Acid-Binding Viruses
title_full Glycosylation of Human IgA Directly Inhibits Influenza A and Other Sialic-Acid-Binding Viruses
title_fullStr Glycosylation of Human IgA Directly Inhibits Influenza A and Other Sialic-Acid-Binding Viruses
title_full_unstemmed Glycosylation of Human IgA Directly Inhibits Influenza A and Other Sialic-Acid-Binding Viruses
title_short Glycosylation of Human IgA Directly Inhibits Influenza A and Other Sialic-Acid-Binding Viruses
title_sort glycosylation of human iga directly inhibits influenza a and other sialic-acid-binding viruses
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5905402/
https://www.ncbi.nlm.nih.gov/pubmed/29617676
http://dx.doi.org/10.1016/j.celrep.2018.03.027
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