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Cell Rep. 2018 Apr 3;23(1):90-99. doi: 10.1016/j.celrep.2018.03.027.
Glycosylation of Human IgA Directly Inhibits Influenza A and Other Sialic-Acid-Binding Viruses.
Maurer MA1, Meyer L1, Bianchi M1, Turner HL2, Le NPL3, Steck M1, Wyrzucki A1, Orlowski V1, Ward AB2, Crispin M4, Hangartner L5.
Author information
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.
KEYWORDS:
IgA; antibodies; glycosylation; heterosubtypic antibodies; immunoglobulin; influenza virus; innate immunity; mucosal immunity; neuraminidase; virus neutralization
PMID: 29617676 DOI: 10.1016/j.celrep.2018.03.027
Glycosylation of Human IgA Directly Inhibits Influenza A and Other Sialic-Acid-Binding Viruses.
Maurer MA1, Meyer L1, Bianchi M1, Turner HL2, Le NPL3, Steck M1, Wyrzucki A1, Orlowski V1, Ward AB2, Crispin M4, Hangartner L5.
Author information
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.
KEYWORDS:
IgA; antibodies; glycosylation; heterosubtypic antibodies; immunoglobulin; influenza virus; innate immunity; mucosal immunity; neuraminidase; virus neutralization
PMID: 29617676 DOI: 10.1016/j.celrep.2018.03.027