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Glycosylation of human IgA directly inhibits influenza A and other sialic-acid-binding viruses

Glycosylation of human IgA directly inhibits influenza A and other sialic-acid-binding viruses
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 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. 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.

antibodies, glycosylation, heterosubtypic antibodies, IgA, immunoglobulin, influenza virus, innate immunity, mucosal immunity, neuraminidase, virus neutralization
2211-1247
90-99
Maurer, Michael A.
b36561be-9f7d-45f1-8f44-bccc928f762a
Meyer, Larissa
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Bianchi, Matteo
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Turner, Hannah L.
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Le, Ngoc P.L.
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Steck, Marco
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Wyrzucki, Arkadiusz
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Orlowski, Vanessa
8eb29589-3c84-495f-a4b5-b7c2f3e2a7c4
Ward, Andrew B.
78ce5b6a-b852-4ee4-a950-f7ff7b183d83
Crispin, Max
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Hangartner, Lars
e2c4669a-bc0e-43e4-a5fe-29581dbf10b3
Maurer, Michael A.
b36561be-9f7d-45f1-8f44-bccc928f762a
Meyer, Larissa
002037fc-efd5-4073-b53c-2e98fed23a6b
Bianchi, Matteo
c064f9c6-7489-4ad2-8511-a2312bf2cda1
Turner, Hannah L.
2a77bdc1-2ac5-40ba-8a50-1f8ee2f568da
Le, Ngoc P.L.
a5b48632-122d-4b3d-8420-69ebded556f1
Steck, Marco
ad6a2638-d267-4eed-8f6d-61e9c79a71d7
Wyrzucki, Arkadiusz
3d0b9345-4156-4545-9019-7212f1ce2420
Orlowski, Vanessa
8eb29589-3c84-495f-a4b5-b7c2f3e2a7c4
Ward, Andrew B.
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Crispin, Max
cd980957-0943-4b89-b2b2-710f01f33bc9
Hangartner, Lars
e2c4669a-bc0e-43e4-a5fe-29581dbf10b3

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 and Hangartner, Lars (2018) Glycosylation of human IgA directly inhibits influenza A and other sialic-acid-binding viruses. Cell Reports, 23 (1), 90-99. (doi:10.1016/j.celrep.2018.03.027).

Record type: Article

Abstract

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. 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.

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Accepted/In Press date: 7 March 2018
e-pub ahead of print date: 5 April 2018
Keywords: antibodies, glycosylation, heterosubtypic antibodies, IgA, immunoglobulin, influenza virus, innate immunity, mucosal immunity, neuraminidase, virus neutralization

Identifiers

Local EPrints ID: 419606
URI: http://eprints.soton.ac.uk/id/eprint/419606
ISSN: 2211-1247
PURE UUID: 1014d574-8192-4b98-b22f-cc84e00f03a0
ORCID for Max Crispin: ORCID iD orcid.org/0000-0002-1072-2694

Catalogue record

Date deposited: 16 Apr 2018 16:30
Last modified: 26 Nov 2021 03:11

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Contributors

Author: Michael A. Maurer
Author: Larissa Meyer
Author: Matteo Bianchi
Author: Hannah L. Turner
Author: Ngoc P.L. Le
Author: Marco Steck
Author: Arkadiusz Wyrzucki
Author: Vanessa Orlowski
Author: Andrew B. Ward
Author: Max Crispin ORCID iD
Author: Lars Hangartner

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